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2 acetyl-CoA + histone H4
2 CoA + diacetylhistone H4
3 acetyl-CoA + histone H4
3 CoA + triacetylhistone H4
-
enzyme form B
mono-, di- and triacetylated products
?
3-azidopropionyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-3-azidopropionyl-L-lysine
3-azidopropionyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-3-azidopropionyl-L-lysine
4 acetyl-CoA + histone H4
4 CoA + tetraacetylhistone H4
-
-
NuA4 randomly acetylates free and nucleosomal H4, with a small preference for lysines 5, 8, and 12 over 16
-
?
4-pentynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-4-pentynoyl-L-lysine
4-pentynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-4-pentynoyl-L-lysine
5-hexynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-5-hexynoyl-L-lysine
5-hexynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-5-hexynoyl-L-lysine
6-heptynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-6-heptynoyl-L-lysine
6-heptynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-6-heptynoyl-L-lysine
acetyl-CoA + 1,4-butanediamine
?
acetyl-CoA + 1,5-pentanediamine
?
acetyl-CoA + 1,6-hexanediamine
?
-
enzyme form A shows low activity , B not
-
-
?
acetyl-CoA + AVDSVFDTILDALK
CoA + AVDSVFDTILDALKac
acetyl-CoA + beta-site amyloid precursor protein-cleaving enzyme 1
CoA + acetylated beta-site amyloid precursor protein-cleaving enzyme 1
acetyl-CoA + biotinylated histone H3 (1-21) peptide
CoA + acetylated biotinylated histone H3 (1-21) peptide
-
-
-
?
acetyl-CoA + c-Myc
CoA + acetylated c-Myc
acetyl-CoA + H3 peptide
?
-
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
acetyl-CoA + histone H
CoA + acetylhistone H
-
histone acetyltransferase AtGCN5 is required to regulate the floral meristem activity through the WUS/AG pathway
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
acetyl-CoA + histone H2A
Nalpha-acetylated-histone H2A + CoA
-
-
-
?
acetyl-CoA + histone H2B
CoA + acetylhistone H2B
acetyl-CoA + histone H3
CoA + acetyl-histone H3
acetyl-CoA + histone H3
CoA + acetylhistone H3
acetyl-CoA + histone H3
peptide CoA + acetylhistone H3 peptide
-
preferred substrate, the N-terminal substrate region plays an importsant role in enhanced affinity of the Gcn5/PCAF proteins for histone H3
-
-
?
acetyl-CoA + histone H3 N-terminal tail
CoA + acetylated histone H3 N-terminal tail
-
50 mM Tris-HCl, pH 8.0, 30°C
-
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
acetyl-CoA + histone H3 peptide
CoA + actylhistone H3
-
residues 1-21 of human histone H3
-
-
?
acetyl-CoA + histone H3 tail peptide
CoA + acetylhistone H3 peptide
H3 peptide substrate, amino acid sequence ARTKQTARKSTGGKAPRKQL
-
-
?
acetyl-CoA + histone H3-peptide
CoA + acetylhistone H3 -peptide
acetyl-CoA + histone H3-peptide
CoA + acetylhistone H3-peptide
acetyl-CoA + histone H3-peptide p19
CoA + acetylhistone H3 -peptide p19
-
-
-
-
?
acetyl-CoA + histone H3-peptide p19
CoA + acetylhistone H3-peptide p19
-
-
-
-
?
acetyl-CoA + histone H3-peptide p20
CoA + acetylhistone H3 -peptide p20
acetyl-CoA + histone H3-peptide p27
CoA + acetylhistone H3 -peptide p27
-
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetyl-CoA + histone H4
Nalpha-acetylated-histone H4 + CoA
acetylation of N-terminal Ser
-
-
?
acetyl-CoA + histone H4
peptide CoA + acetylhistone H4 peptide
acetyl-CoA + histone H4 peptide
CoA + acetylhistone H4 peptide
a synthetic peptide corresponding to the first 20 amino acids of the histone H4 N-terminus
-
-
?
acetyl-CoA + histone H4 peptide
CoA + acetylpeptide of histone H4
residues 1-20 of histone H4
-
-
?
acetyl-CoA + histone H4 peptide
CoA + actylhistone H4
-
residues 2-24 of human histone H4
-
-
?
acetyl-CoA + N-terminal L-lysyl-[beta-catenin]
CoA + H+ + N-terminal Nalpha-acetyl-lysyl-[beta-catenin]
-
-
-
ir
acetyl-CoA + N-terminal L-lysyl-[Hsp70]
CoA + H+ + N-terminal Nalpha-acetyl-L-lysyl-[Hsp70]
acetyl-CoA + NF-kB p65
CoA + acetyl-NF-kB p65
-
acetylation of the subunit at Lys310 by p300 or PCAF
-
-
?
acetyl-CoA + non-histone chromatin high-mobility group protein
CoA + acetylated non-histone chromatin high-mobility group protein
-
or chymotryptic peptides of
-
-
?
acetyl-CoA + p50 protein
CoA + acetyl-p50 protein
acetyl-CoA + p53
CoA + acetyl-p53
acetyl-CoA + p65 protein
CoA + acetyl-p65 protein
acetyl-CoA + peptide H4-20
CoA + acetylpeptide H4-20
-
histone H4-derived peptide substrate
-
-
?
acetyl-CoA + poly-L-lysine
CoA + N6-acetyllysine
-
enzyme form A, not enzyme form B1 and B2
-
?
acetyl-CoA + protamine sulfate
?
acetyl-CoA + protein p53
CoA + acetylprotein p53
acetyl-CoA + putrescine
?
-
-
-
-
?
acetyl-CoA + SGRGKGGKGLGKGGAKRHRK
CoA + SGRGKGGKGLGKGGAKRHR(acK)
-
-
-
?
acetyl-CoA + spermidine
?
acetyl-CoA + transcription factor TFIIE
CoA + acetylated transcription factor TFIIE
-
substrate is a basal transcription factor
-
-
?
acetyl-CoA + transcription factor TFIIF
CoA + acetylated transcription factor TFIIF
-
substrate is a basal transcription factor
-
-
?
acetyl-CoA + VPAFKPGK
CoA + VPAFKPGKac
histone-like protein HBsu peptide
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
acetyl-CoA + [alpha-tubulin]-L-lysine40
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
acetyl-CoA + [AuA]-L-lysine125
CoA + [AuA]-N6-acetyl-L-lysine125
lysine residues at positions 75 and 125 of aurora kinase A (AuA) are acetylated by ARD1, mutational analysis with AUA mutant substrates, overview
-
-
?
acetyl-CoA + [AuA]-L-lysine75
CoA + [AuA]-N6-acetyl-L-lysine75
lysine residues at positions 75 and 125 of aurora kinase A (AuA) are acetylated by ARD1, mutational analysis with AUA mutant substrates, overview
-
-
?
acetyl-CoA + [beta-catenin]-L-lysine
CoA + [beta-catenin]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
acetyl-CoA + [CDC6]-L-lysine
CoA + [CDC6]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [CDC6]-L-lysine14
CoA + [CDC6]-N6-acetyl-L-lysine14
acetyl-CoA + [connexin 43]-L-lysine
CoA + [connexin 43]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
acetyl-CoA + [EGR2]-L-lysine
CoA + [EGR2]-N6-acetyl-L-lysine
acetyl-CoA + [Foxo1]-L-lysine
CoA + [Foxo1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [Geminin]-L-lysine14
CoA + [Geminin]-N6-acetyl-L-lysine14
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
acetyl-CoA + [histone H2A]-L-lysine5
CoA + [histone H2A]-N6-acetyl-L-lysine5
acetyl-CoA + [histone H2B]-L-lysine
CoA + [histone H2B]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H2B]-L-lysine12
CoA + [histone H2B]-N6-acetyl-L-lysine12
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H2B]-L-lysine15
CoA + [histone H2B]-N6-acetyl-L-lysine15
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
acetyl-CoA + [histone H3]-L-lysine13
CoA + [histone H3]-N6-acetyl-L-lysine13
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
acetyl-CoA + [histone H3]-L-lysine18
CoA + [histone H3]-N6-acetyl-L-lysine18
acetyl-CoA + [histone H3]-L-lysine20
CoA + [histone H3]-N6-acetyl-L-lysine20
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine23
CoA + [histone H3]-N6-acetyl-L-lysine23
acetyl-CoA + [histone H3]-L-lysine27
CoA + [histone H3]-N6-acetyl-L-lysine27
acetyl-CoA + [histone H3]-L-lysine56
CoA + [histone H3]-N6-acetyl-L-lysine56
acetyl-CoA + [histone H3]-L-lysine79
CoA + [histone H3]-N6-acetyl-L-lysine79
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
acetyl-CoA + [histone H4]-L-lysin16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
acetyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-acetyl-L-lysine
acetyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-acetyl-L-lysine
acetyl-CoA + [Hsp70]-L-lysine
CoA + [Hsp70]-N6-acetyl-L-lysine
difference in the acetylation of Hsp70 with or without rhARD1 can be observed at low ratio of enzyme: substrate up to 1:25 but not at that of higher ratio over 1:25. The enzyme targets Lys77 of Hsp70, the hARD1/NAA10-mediated catalysis of Hsp70 is abolished with K77R mutation in Hsp70
-
-
?
acetyl-CoA + [MCM2]-L-lysine14
CoA + [MCM2]-N6-acetyl-L-lysine14
acetyl-CoA + [NFkappaB]-L-lysine
CoA + [NFkappaB]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [ORC2]-L-lysine14
CoA + [ORC2]-N6-acetyl-L-lysine14
acetyl-CoA + [p27]-L-lysine
CoA + [p27]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
acetyl-CoA + [PGC-1alpha]-L-lysine
CoA + [PGC-1alpha]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [PGC-1]-L-lysine
CoA + [PGC-1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
acetyl-CoA + [PTEN]-L-lysine
CoA + [PTEN]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 acetylation of the oncosuppressor protein PTEN on two lysine residues (Lys125 and Lys128)
-
-
?
acetyl-CoA + [STAT3]-L-lysine
CoA + [STAT3]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
activated RNA polymerase II transcriptional coactivator p15 + 4-pentynoyl-CoA
?
-
-
-
-
?
alpha-tubulin + acetyl-CoA
acetyl-alpha-tubulin + CoA
androgen receptor + acetyl-CoA
acetylated androgen receptor + CoA
ATM kinase + acetyl-CoA
acetylated ATM kinase + CoA
H4 peptide + acetyl-CoA
?
histone + acetyl-CoA
acetyl-histone + CoA
histone + propionyl-CoA
propionyl-histone + CoA
-
-
-
?
histone H2A + acetyl-CoA
acetyl-histone H2A + CoA
-
acetylation of the tail of the histone, the enzyme is organized in the NuA4 subcomplex acting on the nucleosome, overview
-
-
?
histone H2B + acetyl-CoA
acetyl-histone H2B + CoA
-
acetylation of the tail of the histone, the enzyme is organized in the catalytic Ada2/Ada3/Gcn5 subcomplex of SAGA acting on the nucleosome, overview
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
histone H3 tail peptide + acetyl-CoA
acetyl-histone H3 tail peptide + CoA
-
-
-
-
?
histone H3.2 + 4-pentynoyl-CoA
?
-
-
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
histone H4 N-terminal peptide + acetyl-CoA
acetyl-histone H4 N-terminal peptide + CoA
N-terminal peptide of histone H4 of different length and sequence, prepared in HeLa cell extract, overview, acetylation by Hat1 requires positively charged amino acids at positions 8 and 16 of the H4 tail, substituting glutamine for lysine at Lys8 and Lys16 dramatically reduces the ability of yHat1p to acetylate the H4 tail peptide, phosphorylation of Ser1 also reduces the acetylation of H4 peptides
-
-
?
isoform 1 of DNA polymerase zeta catalytic subunit + 4-pentynoyl-CoA
?
-
-
-
-
?
isoform 1 of transcription factor BTF3 + 4-pentynoyl-CoA
?
-
-
-
-
?
isoform 2 of protein SET + 4-pentynoyl-CoA
?
-
-
-
-
?
isoform long of antigen KI-67 + 4-pentynoyl-CoA
?
-
-
-
-
?
nucleolin + 4-pentynoyl-CoA
?
-
-
-
-
?
piccoloNuA4 peptide + acetyl-CoA
acetyl-piccoloNuA4 peptide + CoA
the peptide is part of the physiologic enzme complex, overview
-
-
?
piccoloNuA4 peptide + propionyl-CoA
propionyl-piccoloNuA4 peptide + CoA
-
-
-
?
promyelotic leukemia zinc finger gene + acetyl-CoA
acetylated promyelotic leukemia zinc finger gene + CoA
additional information
?
-
2 acetyl-CoA + histone H4
2 CoA + diacetylhistone H4
-
-
mono-, di- and triacetylated products
?
2 acetyl-CoA + histone H4
2 CoA + diacetylhistone H4
-
enzyme form B
mono- and diacetylated products
?
2 acetyl-CoA + histone H4
2 CoA + diacetylhistone H4
-
enzyme form B
mono- and diacetylated products
?
3-azidopropionyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-3-azidopropionyl-L-lysine
-
-
-
?
3-azidopropionyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-3-azidopropionyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
3-azidopropionyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-3-azidopropionyl-L-lysine
-
-
-
?
3-azidopropionyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-3-azidopropionyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
4-pentynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-4-pentynoyl-L-lysine
-
-
-
?
4-pentynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-4-pentynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
4-pentynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-4-pentynoyl-L-lysine
-
-
-
?
4-pentynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-4-pentynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
5-hexynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-5-hexynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
5-hexynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-5-hexynoyl-L-lysine
very low activity with 5-hexynoyl-CoA
-
-
?
5-hexynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-5-hexynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
5-hexynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-5-hexynoyl-L-lysine
very low activity with 5-hexynoyl-CoA
-
-
?
6-heptynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-6-heptynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
6-heptynoyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-6-heptynoyl-L-lysine
very low activity with 6-heptynoyl-CoA
-
-
?
6-heptynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-6-heptynoyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
6-heptynoyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-6-heptynoyl-L-lysine
very low activity with 6-heptynoyl-CoA
-
-
?
acetyl-CoA + 1,4-butanediamine
?
-
enzyme form A and B, low activity
-
-
?
acetyl-CoA + 1,4-butanediamine
?
-
i.e. putrescine
-
-
?
acetyl-CoA + 1,5-pentanediamine
?
-
enzyme form A and B, low activity
-
-
?
acetyl-CoA + 1,5-pentanediamine
?
-
i.e. cadaverine
-
-
?
acetyl-CoA + AVDSVFDTILDALK
CoA + AVDSVFDTILDALKac
histone-like protein HBsu peptide
-
-
?
acetyl-CoA + AVDSVFDTILDALK
CoA + AVDSVFDTILDALKac
histone-like protein HBsu peptide
-
-
?
acetyl-CoA + beta-site amyloid precursor protein-cleaving enzyme 1
CoA + acetylated beta-site amyloid precursor protein-cleaving enzyme 1
-
-
-
-
?
acetyl-CoA + beta-site amyloid precursor protein-cleaving enzyme 1
CoA + acetylated beta-site amyloid precursor protein-cleaving enzyme 1
-
50 mM Tris-HCl, pH 8.0, 30°C
-
-
?
acetyl-CoA + c-Myc
CoA + acetylated c-Myc
-
acetylation by Tip60 increases c-Myc protein stability in transfected H-1299 human lung carcinoma cells
-
-
?
acetyl-CoA + c-Myc
CoA + acetylated c-Myc
-
acetylation by Tip60
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
Artemia nauplii
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H1 is a better substrate than H3 or H4
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
important role of the enzyme for chromatin modulating activity
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
Betapolyomavirus macacae
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
enzyme form B nearly exclusively acetylates histones H4 and H2a
formation of N6-acetyllysine as the only acetylation product
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
or chymotryptic peptides of histone
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
most likely involved in acetylation of newly synthesized histones in cytoplasm prior to chromatin assembly
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
ir
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
in the assay the CoA thiolate is detected by the thiol sensitive fluorescent dye 7-diethylamino-3-(4'-maleimidylphenyl)-4-methylcoumarin
-
?
acetyl-CoA + histone
CoA + acetylhistone
calf thymus and HeLa cell histones
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H1 is not acetylated in vivo
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
involved in chromatin remodeling and DNA repair
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H1 is not acetylated in vivo
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
ir
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
involved in chromatin remodeling and DNA repair
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
acetylates histones H2A, H3, and H4, but not histone 2B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
the bifunctional enzyme NCOAT, nuclear cytoplasmic O-GlcNacase and acetyltransferase, may be regulated to reduce the state of glycosylation of transcriptional activators while increasing the acetylation of histones to allow for concerted activation of eukaryotic gene transcription
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H2A is a substrate for enzyme form A1
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H2B: poor substrate for enzyme form A2
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
involved in dynamic equilibrium of core histone acetylation
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
pea histones, enzyme form A and B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
chicken erythrocyte histones, enzyme form A and B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
free pea and chicken histones H4, enzyme form B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
acetylation of lysine 5, 8, 12, and 16 of free histone H4 with increasing preference
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
free histones
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
free histones
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
nucleosome-histones, enzyme form A, not enzyme form B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone f1, enzyme form A
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone f2a1, enzyme form B1 and B2
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
nucleosome-histones, enzyme form A and B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H1 poor substrate
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
chicken erythrocyte histones, enzyme form A and B
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
Esa1 protein is involved in cell cycle regulation
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
involved in chromatin remodeling and DNA repair
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone acetylation on Lys16 by Sas2
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
a group of enzymes with differing specificity towards histone acceptors, specificity of different enzyme forms
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
chymostatic peptides of histones
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
histone H1 is a better substrate than H3 or H4
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
histone H1 poor substrate
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
acetylation of histone H1 only in vitro
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
histone H1 poor substrate
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
acetylation of histone H1 only in vitro
-
-
?
acetyl-CoA + histone H1
CoA + acetylhistone H1
-
histone H1 poor substrate
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
-
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
enzyme form B nearly exclusively acetylates histones H4 and H2a
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
MYST-related histone acetyltransferase complex Tip60
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
acetylation at Lys5 by Tip60
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
-
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
-
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
histone H2A is a substrate for enzyme form A1
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
NuA4-like protein acetylates histone H4 and H2A
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
NuA4-like protein acetylates histone H4 and H2A
-
?
acetyl-CoA + histone H2B
CoA + acetylhistone H2B
-
-
-
?
acetyl-CoA + histone H2B
CoA + acetylhistone H2B
-
GNAT-related histone acetyltransferase complexes STAGA or TFTC
-
-
?
acetyl-CoA + histone H2B
CoA + acetylhistone H2B
-
histone H2B: poor substrate for enzyme form A2
-
?
acetyl-CoA + histone H2B
CoA + acetylhistone H2B
-
-
-
?
acetyl-CoA + histone H2B
CoA + acetylhistone H2B
-
histone H2B: preferred substrate of enzyme form A
-
?
acetyl-CoA + histone H2B
CoA + acetylhistone H2B
-
GNAT-related histone acetyltransferase complexes SAGA, ADA or H2B
-
-
?
acetyl-CoA + histone H3
CoA + acetyl-histone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetyl-histone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
residues K14, K18, and K23 of H3 are acetylated by domain C1 of isoform Idm1 in vitro
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: preferred substrate, acetylation at Lys14
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys9
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys14 of histone H3
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H1 is a better substrate than H3 or H4
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: preferred substrate, acetylation at Lys14
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys9, Lys14, Lys18, Lys23, Lys27, Lys36, and Lys37
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys9
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
PCAF protein
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: preferred substrate, acetylation at Lys14
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Lys14 of histone H3 and a peptide containing Lys14 thereof are the preferred substrates for Gnc5 and PCAF protein, as well as Gnc5 and PCAF catalytic domain
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Lys14 of histone H3 and a peptide containing Lys14 thereof are the preferred substrates for Gnc5 and PCAF protein, as well as Gnc5 and PCAF catalytic domain
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
GNAT-related histone acetyltransferase complexes PCAF, STAGA or TFTC
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
substrate is a H3 peptide
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
the sequence G-K-X-P within histone H3 makes several key contacts within the active site that are conserved in GNAT members including p/CAF
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys18
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
acetylation of Lys23
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
PCAF protein
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys4 and Lys9
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
regulation, detailed overview. Acetylation and deacetylation events, in combination with other post-translational protein modifications, generate an NF-kappaB-signaling code and regulate NF-kappaB-dependent gene transcription in an inducer- and promoter-dependent manner, overview
-
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: preferred substrate, acetylation at Lys14
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
CBP binds and acetylates histones at neural promoters, and regulates Corpus Callosum development. CBP binds to neuronal and glial promoters and globally promotes histone acetylation in the embryonic cortex, e.g. the beta-actin promoter, overview
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
H4R3 methylation, catalyzed by PRMT1, facilitates beta-globin transcription by regulating histone acetyltransferase binding, and histone H3 and H4 acetylation, overview
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys9 and Lys14
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys9 and Lys14 by PCAF. PCAF binds to dimethyl-Arg3 at histone H4 tails, dimethyl H4R3 provides a binding surface for PCAF and directly enhances histone H3 and H4 acetylation in vitro
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H3 is the preferred substrate of enzyme form A1 and A2
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H3: preferred substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: specific for Lys14 of histone H3
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Gcn5 protein: preferred substrate, acetylation at Lys14
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H3: preferred substrate
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H3 preferred substrate of enzyme form A
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
recombinant and native SAS complex acetylates Lys14
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
GNAT-related histone acetyltransferase complexes SAGA, ADA or HAT-A2, MYST-related histone acetyltransferase complex NuA3
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
strong preference for free histones relative to chromatin substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Rtt109 association with distinct histone chaperones directs substrate selection between N-terminal lysines, H3K9, H3K23, and those within the histone fold domain, H3K56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Rtt109 is specific for histone H3, acetylation at Lys9 and Lys56. RTT109 has functions in addition to maintaining genome stability
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Rtt109 association with distinct histone chaperones directs substrate selection between N-terminal lysines, H3K9, H3K23, and those within the histone fold domain, H3K56. The sequence G-K-X-P within histone H3, which includes the primary Gcn5 substrate K14, makes several key contacts within the active site that are conserved with other GNAT members
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Rtt109 is specific for histone H3, acetylation at Lys9 and Lys56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys18
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
histone H3: preferred substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
the sequence G-K-X-P within histone H3, which includes the primary Gcn5 substrate K14, makes several key contacts within the active site that are conserved in GNAT members
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
the sequence G-K-X-P within histone H3, which includes the primary Gcn5 substrate K14, makes several key contacts within the active site that are conserved in GNAT members
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys14 by tGCN5 in the consensus sequence QTARKSTGGK14APRKLASK
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys14 by tGCN5 in the consensus sequence QTARKSTGGK14APRKLASK. Phe125 and Phe164 interact with the substrate, but are not directly involved in the acetylation reaction, while residues Glu122, Val123 and Tyr160 are critical for catalysis
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
preferred substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
preferred substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
enzyme form B, very low activity
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
enzyme form B, very low activity
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
Lys14 of histone H3 and a peptide containing Lys14 thereof are the preferred substrates for Gnc5 and PCAF protein, as well as Gnc5 and PCAF catalytic domain
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
Lys14 of histone H3 and a peptide containing Lys14 thereof are the preferred substrates for Gnc5 and PCAF protein, as well as Gnc5 and PCAF catalytic domain
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptides H3p19, H3p27, H3p11 are substrates for the catalytic domain of Gcn5 and PCAF
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptides H3p19, H3p27, H3p11 are substrates for the catalytic domain of Gcn5 and PCAF
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
Lys14 of histone H3 and a peptide containing Lys14 thereof are the preferred substrates for Gnc5 and PCAF protein, as well as Gnc5 and PCAF catalytic domain
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptides H3p19, H3p27, H3p11 are substrates for the catalytic domain of Gcn5 and PCAF
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptides H3p19, H3p27, H3p11 are substrates for the catalytic domain of Gcn5 and PCAF
-
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptides H3p19, H3p27, H3p11 are substrates for the catalytic domain of Gcn5 and PCAF
-
-
?
acetyl-CoA + histone H3 peptide
CoA + acetylhistone H3 peptide
-
peptide H3p20
-
-
?
acetyl-CoA + histone H3-peptide
CoA + acetylhistone H3 -peptide
-
-
-
-
?
acetyl-CoA + histone H3-peptide
CoA + acetylhistone H3 -peptide
-
-
-
-
?
acetyl-CoA + histone H3-peptide
CoA + acetylhistone H3 -peptide
-
-
-
-
?
acetyl-CoA + histone H3-peptide
CoA + acetylhistone H3-peptide
-
-
-
-
?
acetyl-CoA + histone H3-peptide
CoA + acetylhistone H3-peptide
-
-
-
-
?
acetyl-CoA + histone H3-peptide p20
CoA + acetylhistone H3 -peptide p20
-
-
-
-
?
acetyl-CoA + histone H3-peptide p20
CoA + acetylhistone H3 -peptide p20
-
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Gcn5 protein acetylates H4 when purified and presented separately to the enzyme at Lys8 and Lys16
-
r
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys14
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
RmtA is specific for histone H4 with Arg3 as the methylation site. Methylation of histone H4 by recombinant RmtA affects the acetylation by p300/CBP, supporting aninterrelation of histone methylation and acetylation in transcriptional regulation. Important role of the enzyme for chromatin modulating activity
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
RmtA is specific for histone H4 with Arg3 as the methylation site
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B nearly exclusively acetylates histones H4 and H2a
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
highly specific for
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Gcn5 protein acetylates H4 when purified and presented separately to the enzyme at Lys8 and Lys16
-
r
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4: all of the acetate groups are introduced within the NH2-terminal amino acids 4 to 17
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys16 by MYST1 is essential for chromatin remodeling and is used for regulation of gene expression in eukaryotes. The nucleosome is a disc-shaped octamer consisting of two heterotetramers formed by histones H3/H4 and histones H2A and H2B
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Mof is required for sex chromosome dosage compensation acting in the MSL complex, which also contains Msl1-3, Mle, and RNA, to acetylate H4K16 and to increase gene transcription from the single male X chromosome
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys16 by MYST1
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation of Lys5, Lys8, Lys12, and Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Hat1 is a primary enzyme for di-acetylating cytosolic histone H4 at Lys5 and Lys12 in the cytosol
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys14
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Gcn5 protein acetylates H4 when purified and presented separately to the enzyme at Lys8 and Lys16
-
r
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
PCAF protein
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is the preferred substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
histone H4 is the preferred substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
specific acetylation of Lys16, reversible acetylation of histones play an important role in regulation of chromatin structure and function. HMOF has a role in DNA damage responseduring cell cycle progression
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
MYST-related histone acetyltransferase complex Tip60, GNAT-related histone acetyltransferase complex PCAF
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
HBO1 is an H4-specific histone acetylase, and is a coactivator of the DNA replication licensing factor Cdt1. HBO1 acetylase activity is essential for DNA licensing of replication origins, where it controls H4 acetylation at the origins. H4 acetylation at origins is cell-cycle regulated, with maximal activity at the G1/S transition
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
HBO1 regulates global histone H4 acetylation
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
MSL-associated MOF acetylates nucleosomal histone H4 almost exclusively on Lys16, while NSL-associated MOF exhibits a relaxed specificity and also acetylates nucleosomal histone H4 on Lys5 and Lys8
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
MYST1 specificity to Lys16 of histone H4 is not absolute, because in experiments in vitro the protein is also able to acetylate histones H3 and H2A, whereas in vivo only modification of histone H4 is specific. Acetylation at Lys16 by MYST1 is essential for chromatin remodeling and is used for regulation of gene expression in eukaryotes. The nucleosome is a disc-shaped octamer consisting of two heterotetramers formed by histones H3/H4 and histones H2A and H2B. All human autosomes are susceptible to histone H4 acetylation by Lys16 residue and acetyltransferase MYST1
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation at Lys16 by MYST1
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
activity with synthetic histone H4 tail peptide substrate of p300 that shows different degrees of autoacetylation, overview. Tyr1467 appears to serve as a general acid protonating the departing coenzyme A sulfur
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
recombinant ATAC2 has a weak HAT activity directed to histone H4
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
recombinant Hbo1 can acetylate nucleosomal histone H4 in vitro, with a preference for Lys5 and Lys12, mapping of acetylation sites, overview
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
substrate is a H4 peptide
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
substrate is H4 peptide
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation of Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation of Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation of Lys16
in the assay the CoA thiolate is detected by the thiol sensitive fluorescent dye 7-diethylamino-3-(4'-maleimidylphenyl)-4-methylcoumarin
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
the enzyme PCAF acetylates histone H4 at lysine 8
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is the preferred substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
PCAF protein
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
H4R3 methylation, catalyzed by PRMT1, facilitates beta-globin transcription by regulating histone acetyltransferase binding, and histone H3 and H4 acetylation, overview
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Mof is solely responsible for H4K16 acetylation in mouse blastocysts. Tip60 plays essential roles in cell cycle progression in vitro
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
PCAF binds to dimethyl-Arg3 at histone H4 tails, dimethyl H4R3 provides a binding surface for PCAF and directly enhances histone H3 and H4 acetylation in vitro
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
recombinant ATAC2 has a weak HAT activity directed to histone H4
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B is specific for histone H4
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
highly specific for
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B
mono-, di- and triacetylated products
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylates histone H4 in vitro at K5, K8, K12 and K16
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B is specific for histone H4
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is a poor substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Gcn5 protein acetylates H4 when purified and presented separately to the enzyme at Lys8 and Lys16
-
r
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
NuA4-like protein acetylates histone H4 and H2A
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
SAS complex, native and recombinant, acetylates Lys16
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B has a marked specificity for histone H4
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is the preferred substrate
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is the preferred substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
histone H4 is the preferred substrate
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation of histone H4 by NuA4 is required for the cellular resistance to spindle stress. The NuA4 histone acetyltransferase subunit Yaf9, is required for the cellular response to spindle stress in yeast
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
exclusively acetylates of Lys16 of histone H4, the enzyme is required for bulk of H4 lysine 16 acetylation in vivo, role of SAS complex in antagonizing the speading of Sir proteins at silent loci in Saccharomyces cerevisiae
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
the level of HAT-B-dependent acK12H4 may be very low under normal growth condition
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetyltion of Lys16, acetylates free histones and weakly acetylates nucleosomes
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
MYST-related histone acetyltransferase complex NuA4 or SAS(SAS-I)
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
specifically acetylates Lys12, and to a lesser extent Lys5 of free, non-chromatin-bound histone H4
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
both Lys12 and Lys5 of soluble, non-chromatin-bound histone H4 are in vivo targets of acetylation for the yeast HAT-B enzyme. Lys12/Lys5-acetylated histone H4 is bound to the HAT-B complex in the soluble cell fraction. Exchange of Lys for Arg at position 12 of histone H4 do not interfere with histone H4 association with the complex, but prevented acetylation on Lys5 by the HAT-B enzyme, in vivo as well as in vitro
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
full-length histone H4 is acetylated 2000fold faster than histone tail peptides
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
substrates are synthetic N-terminal H4 peptides. The HAT-B complex acetylates only Lys12, recombinant Hat1 is able to modify Lys12 and Lys5. Exchange of Lys for Arg at position 12 of histone H4 does not interfere with histone H4 association with the complex, but prevents acetylation on Lys5 by the HAT-B enzyme, in vivo as well as in vitro
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
r
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
NuA4-like protein acetylates histone H4 and H2A
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B
mono- and diacetylated products
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
enzyme form B
mono- and diacetylated products
?
acetyl-CoA + histone H4
peptide CoA + acetylhistone H4 peptide
-
specific acetylation of Lys16
-
-
?
acetyl-CoA + histone H4
peptide CoA + acetylhistone H4 peptide
-
-
-
?
acetyl-CoA + N-terminal L-lysyl-[Hsp70]
CoA + H+ + N-terminal Nalpha-acetyl-L-lysyl-[Hsp70]
-
-
-
ir
acetyl-CoA + N-terminal L-lysyl-[Hsp70]
CoA + H+ + N-terminal Nalpha-acetyl-L-lysyl-[Hsp70]
acetylation of residue K77
-
-
ir
acetyl-CoA + p50 protein
CoA + acetyl-p50 protein
-
acetylation of p50 by p300 independent of shear stress
-
-
?
acetyl-CoA + p50 protein
CoA + acetyl-p50 protein
-
acetylation of histones H4 at the site of SSRE within the eNOS promoter
-
-
?
acetyl-CoA + p53
CoA + acetyl-p53
p53 protein-acetylation of the Lys120 residue
-
-
?
acetyl-CoA + p53
CoA + acetyl-p53
p53 protein-acetylation of the Lys120 residue is carried out by acetyltransferases MYST1 and TIP60 to approximately equal extent
-
-
?
acetyl-CoA + p65 protein
CoA + acetyl-p65 protein
-
acetylation of p65 by p300 during translocation into the nuclei in response to shear stress
-
-
?
acetyl-CoA + p65 protein
CoA + acetyl-p65 protein
-
acetylation of histones H3 at the site of SSRE within the eNOS promoter
-
-
?
acetyl-CoA + protamine sulfate
?
-
enzyme form A, not enzyme form B
-
-
?
acetyl-CoA + protamine sulfate
?
-
enzyme form A, not enzyme form B
-
-
?
acetyl-CoA + protein p53
CoA + acetylprotein p53
-
-
-
-
r
acetyl-CoA + protein p53
CoA + acetylprotein p53
-
-
-
?
acetyl-CoA + protein p53
CoA + acetylprotein p53
-
substrate is a DNA-binding transcription activator and a tumor suppressor
-
-
?
acetyl-CoA + protein p53
CoA + acetylprotein p53
-
peptide of p53 is a substrate for PCAF catalytic domain
-
-
?
acetyl-CoA + spermidine
?
-
-
-
-
?
acetyl-CoA + spermidine
?
-
-
-
-
?
acetyl-CoA + spermidine
?
-
enzyme form B, not enzyme form A
-
-
?
acetyl-CoA + spermidine
?
-
-
-
-
?
acetyl-CoA + spermine
?
-
-
-
-
?
acetyl-CoA + spermine
?
-
-
-
-
?
acetyl-CoA + spermine
?
-
enzyme form A inactive, enzyme form B active
-
-
?
acetyl-CoA + spermine
?
-
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine40
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine40
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
KAT2A acetylates Lys40 of TUBA
-
-
?
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [CDC6]-L-lysine14
CoA + [CDC6]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [CDC6]-L-lysine14
CoA + [CDC6]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [EGR2]-L-lysine
CoA + [EGR2]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [EGR2]-L-lysine
CoA + [EGR2]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [Geminin]-L-lysine14
CoA + [Geminin]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [Geminin]-L-lysine14
CoA + [Geminin]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
essential histone-like protein HBsu contains seven acetylation sites in vivo, mutational analysis using mutants hbsK86Q, hbsK41Q, hbsK3Q, hbsK41R, and hbsK37R
-
-
?
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
histone-like protein HBsu
-
-
?
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
essential histone-like protein HBsu contains seven acetylation sites in vivo, mutational analysis using mutants hbsK86Q, hbsK41Q, hbsK3Q, hbsK41R, and hbsK37R
-
-
?
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
histone-like protein HBsu
-
-
?
acetyl-CoA + [histone H2A]-L-lysine5
CoA + [histone H2A]-N6-acetyl-L-lysine5
-
-
-
-
ir
acetyl-CoA + [histone H2A]-L-lysine5
CoA + [histone H2A]-N6-acetyl-L-lysine5
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine18
CoA + [histone H3]-N6-acetyl-L-lysine18
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine18
CoA + [histone H3]-N6-acetyl-L-lysine18
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H3]-L-lysine23
CoA + [histone H3]-N6-acetyl-L-lysine23
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine23
CoA + [histone H3]-N6-acetyl-L-lysine23
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine27
CoA + [histone H3]-N6-acetyl-L-lysine27
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine27
CoA + [histone H3]-N6-acetyl-L-lysine27
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine56
CoA + [histone H3]-N6-acetyl-L-lysine56
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine56
CoA + [histone H3]-N6-acetyl-L-lysine56
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine56
CoA + [histone H3]-N6-acetyl-L-lysine56
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
-
ir
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
-
ir
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
main substrate
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
-
ir
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 main substrate
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
-
ir
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
-
ir
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
?
acetyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone peptide H3-20]-L-lysine
CoA + [histone peptide H3-20]-N6-acetyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
acetyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone peptide H4-20]-L-lysine
CoA + [histone peptide H4-20]-N6-acetyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
acetyl-CoA + [MCM2]-L-lysine14
CoA + [MCM2]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [MCM2]-L-lysine14
CoA + [MCM2]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [ORC2]-L-lysine14
CoA + [ORC2]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [ORC2]-L-lysine14
CoA + [ORC2]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
-
-
-
?
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
-
ir
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
substrate of wild-type enzyme GCN5 and enzyme mutant T612G
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
endogenous GCN5 and EGR2 in iNKT cells
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
endogenous GCN5 and EGR2 in iNKT cells
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
alpha-tubulin + acetyl-CoA
acetyl-alpha-tubulin + CoA
-
-
-
-
?
alpha-tubulin + acetyl-CoA
acetyl-alpha-tubulin + CoA
-
-
-
-
?
androgen receptor + acetyl-CoA
acetylated androgen receptor + CoA
-
receptor signaling in prostate cancer cells is augmented by the androgen receptor coactivator p300, which transactivates and acetylates the androgen receptor in the presence of 100 nM dihydrotestosterone, involvement of p300 in neuropeptide activation of androgen receptor signaling, overview
-
-
?
androgen receptor + acetyl-CoA
acetylated androgen receptor + CoA
-
the KLKK motif of androgen receptor protein is both necessary and sufficient for acetylation by p300 in the presence of 100 nM dihydrotestosterone
-
-
?
ATM kinase + acetyl-CoA
acetylated ATM kinase + CoA
-
ATM protein kinase regulates the cells response to DNA damage through the phosphorylation of proteins involved in cell-cycle checkpoints and DNA repair, suppression of Tip60 blocks the activation of ATMs kinase activity, ATM autophosphorylation e.g. at Ser1981, and prevents the ATM-dependent phosphorylation of p53 and chk2, inactivation of Tip60 sensitizes cells to ionizing radiation, overview
-
-
?
ATM kinase + acetyl-CoA
acetylated ATM kinase + CoA
-
the ataxia telangiectasia mutant, i.e. ATM, protein kinase, ATM forms a stable complex with Tip60 through the conserved, highly required FATC domain of ATM, the interaction between ATM and Tip60 is not regulated in response to DNA damage, but is specifically induced by DNA damage, overview, mutations in the FATC domain that abolish the interaction between ATM and Tip60
-
-
?
H4 peptide + acetyl-CoA
?
-
-
-
-
?
H4 peptide + acetyl-CoA
?
-
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
-
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
histone acetylation is an important posttranslational modification correlated with gene activation, the HAC1 is involved in the regulation of flowering time via repression of flowering locus C, the enzyme participates in many physiological processes, including proliferation, differentiation, and apoptosis
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
-
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
phosphorylation of p300 at Ser1834 by the kinase Akt is essential for its histone acetyltransferase and transcriptional activity
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
histones from the Hela cell core
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
key enzyme in post-translational modification of histones associated with transcriptionally active genes
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation of Lys9, and Lys14
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
-
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation of Lys9, and Lys14
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
regulation
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
the enzyme is involved in ethanol-induced acetylation of histone H3 in hepatocytes, potential mechanism for gene expression activation by the enzyme, overview
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation at Lys9
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation at Lys9 and Lys14
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
-
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation of the tail of the histone, the enzyme is organized in the catalytic Ada2/Ada3/Gcn5 subcomplex of SAGA acting on the nucleosome, overview
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
acetylation of Lys5, Lys8, and Lys12, Gcn5 and transcriptional adaptor Ada2a are involved in nucleosomal histone H4 acetylation
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
acetylation of Lys5, Lys8, and Lys12
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
-
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
acetylation of Lys5, Lys8, and Lys12
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
-
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
acetylation at Lys8, NCOAT has the ability to directly associate with both an acetylated and unacetylated histone H4 tail in vitro without tequiring acetyl-lysine contacts, binding and interaction mechanism, overview
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
acetylation of the tail of the histone, the enzyme is organized in the NuA4 subcomplex acting on the nucleosome, overview
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
acetylation at Lys5 and Lys12, acetylation by Hat1 requires positively charged amino acids at positions 8 and 16 of the H4 tail
-
-
?
promyelotic leukemia zinc finger gene + acetyl-CoA
acetylated promyelotic leukemia zinc finger gene + CoA
-
-
-
-
?
promyelotic leukemia zinc finger gene + acetyl-CoA
acetylated promyelotic leukemia zinc finger gene + CoA
-
i.e. PLZF, a direct and specific substrate of the p300 HAT, no activity with the substrate deletion mutant lacking zinc fingers 6 to 9
-
-
?
additional information
?
-
-
Gcn5 is a coactivator of transcription
-
-
?
additional information
?
-
-
Gcn5 and PCAF protein are transcription cofactors
-
-
?
additional information
?
-
-
affects the inflorescence meristem and stamen development in Arabidopsis thaliana
-
-
?
additional information
?
-
-
histone acetylation and deacetylation is an epigenetic mechanism in volved in regulation of mIRNA production. GCN5 has a general repressive effect on microRNAs, miRNAs, and it targets a subset of MIRNA genes, GCN5 is required for acetylation of histone H3 lysine 14 at these loci, overview
-
-
?
additional information
?
-
isoform GCN5 is not the enzyme responsible for histone acetylation at cold-regulated genes COR promoters during cold acclimation
-
-
?
additional information
?
-
-
GCN5 directly targets HSFA3 and UVH6 and affects their H3K9 and H3K14 acetylation levels
-
-
?
additional information
?
-
quantification of HBsu acetylation by parallel reaction monitoring-tandem mass spectrometry
-
-
-
additional information
?
-
quantification of HBsu acetylation by parallel reaction monitoring-tandem mass spectrometry
-
-
-
additional information
?
-
-
protamine, bovine serum albumin, and ubiquitin are no substrates
-
-
?
additional information
?
-
-
Tip60, in complex with homologues of the mammalian Tip60 complex, exhibits functional redundancy with two other groups of genes, known as synthetic multivulva A and B genes, synMUV. Therefore, the genes encoding proteins of the Tip60 complex are termed class C synMUV genes. SynMUV A and B counteract EGF to Ras to MAPK signaling and the Tip60 complex is a chromatin-modifying complex
-
-
?
additional information
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a homologue of Moz, zMoz, occurs in zebrafish to perform a potential Moz function in the trunk region
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?
additional information
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a homologue of Moz, zMoz, occurs in zebrafish to perform a potential Moz function in the trunk region
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?
additional information
?
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Gcn5 is a coactivator of transcription
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additional information
?
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Gcn5 and PCAF protein are transcription cofactors
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?
additional information
?
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the enzyme plays a role in chromatin structure and gene expression regulation as a catalytic component of multiprotein complexes, some of which also contain Ada2-type transcriptional coactivators
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?
additional information
?
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MYST1 is a part of multiprotein complexes that accomplish functions of male X chromosome activation and thereby functions of dosage compensation in Drosophila and, in mammals, global acetylation of histone H4 K16. Functional links between MYST1 and proteins ATM and p53. Interactions between MSL1 and MYST1 within the MSL complex in Drosophila melanogaster, the compensasome includes proteins MSL1, MSL2, MSL3, MLE, MOF, a histone acetyltransferase homologous to MYST1, JIL1, and two non-coding RNA: roX1 and roX2, structure and function of the compensasome, detailed overview. Cell interactome fragments including protein homologs of hampin and MYST1, overview
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?
additional information
?
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histones H3 and H4 and their chaperone Asf1, including RbAp48, a regulatory subunit of Hat1 enzyme, are associated with Hat1 in the cytosol of chicken cells. Hat1 regulates integrity of cytosolic histone H3-H4 containing complex, effect of Hat1 on status for the cytosolic histones H3/H4 pre-deposition complexes with respective chaperone proteins, overview
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additional information
?
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Gcn5 is a coactivator of transcription
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?
additional information
?
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Gcn5 and PCAF protein are transcription cofactors
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?
additional information
?
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Gcn5 and PCAF protein are transcription cofactors
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?
additional information
?
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Gcn5 and PCAF protein are transcription cofactors
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?
additional information
?
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Gcn5 and PCAF protein are transcription cofactors
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?
additional information
?
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enzyme activity is regulated by phosphorylation and interaction with other regulating protein factors
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?
additional information
?
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MOZ and MORF genes are rearranged by chromosome abnormalities associated with several types of leukemia
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additional information
?
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MYST-related histone acetyltransferase complex Tip60 also acts as a transcriptional coactivator in several systems including class I nuclear hormone receptors, NF-kappaB and at the superoxide dismutase gene. Tip 60 has been implicated in Alzheimer disease because it stimulates transcription when asociated with the cleaved cytoplasmic tail fragment of the amyloid-beta precursor protein
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additional information
?
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Tip60 plays a role in the control of cell-related events
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additional information
?
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acetylation of proteins by the enzyme plays a critical role in the regulation of gene expression
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additional information
?
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androgen Src kinase and PKCd kinase are involved in the regulation of p300 HAT activity via bombesin, overview
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?
additional information
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deregulated HAT activity plays a role in the development of a range of cancers
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additional information
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the enzyme is involved in Sp1 activation of the cyclin D1 promoter, TAF1-dependent histone acetylation facilitates transcription factor binding to the Sp1 sites, thereby activating cyclin D1 transcription and ultimately G1-to-S-phase progression, regulation, overview
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?
additional information
?
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the histone acetyltransferase activity of p300 is required for transcriptional repression by the promyelocytic leukemia zinc finger protein
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additional information
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in absence of acceptor substrate the enzyme performs autoacetylation, identification of 13 autoacetylation sites and mechanism, autoacetylation catalyzed by p300 HAT is about 1000-fold more efficient than p300/CREB-binding protein-associated factor-mediated acetylation of catalytically defective p300 HAT, overview
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?
additional information
?
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ATAC2 associates with GCN5 and other proteins linked to chromatin metabolism
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additional information
?
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besides the male-specific lethal, MSL, HAT complex, MOF is also a component of the second HAT complex, designated the non-specific lethal, NSL complex, substrate specificity of the NSL complex, overview. Assembly of the MOF HAT into MSL or NSL complexes controls its substrate specificity
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additional information
?
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besides the male-specific lethal, MSL, HAT complex, MOF is also a component of the second HAT complex, designated the non-specific lethal, NSL complex, substrate specificity of the NSL complex, overview. Assembly of the MOF HAT into MSL or NSL complexes controls its substrate specificity
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?
additional information
?
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HBO1 histone acetylase is involved in DNA replication licensing and associates with replication origins, located within the HPRT1 coding sequence, specifically during the G1 phase of the cell cycle in a manner that depends on the replication licensing factor Cdt1, but is independent of the Cdt1 repressor geminin
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?
additional information
?
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HBO1 occurs as a component of a multiprotein complex with histone H3 and H4 acetyltransferase activity in 293 cells. The mammalian complex corresponding to the yeast NuA4 complex contains the MYST HAT Tip60
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?
additional information
?
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in response to DNA damage, Tip60 acetylates ATM, a DNA damage related kinase, allowing for phosphorylation of Chk2 and p53 by ATM. HATs perform a conserved mechanism of acetyl-transfer, where the lysine-containing substrate directly attacks enzyme-bound acetyl-CoA. The ability of HATs to form distinct multi-subunit complexes provide a means to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex
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?
additional information
?
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increase in eNOS mRNA, caused by shear stress, is completely blocked by pharmacological inhibition of p300/HAT activity with curcumin or by p300 small interfering RNA
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?
additional information
?
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mechanistically, p300 acts as a transcriptional coactivator through the direct interaction with a diverse set of transcription factors and RNA polymerase II transcription machinery
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?
additional information
?
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MYST1 is a part of multiprotein complexes that accomplish functions of male X chromosome activation and thereby functions of dosage compensation in Drosophila and, in mammals, global acetylation of histone H4 K16. Functional links between MYST1 and proteins ATM and p53. MYST1 interacts with WDR5. Cell interactome fragments including protein homologs of hampin and MYST1, overview
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?
additional information
?
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Tip60 is part of the evolutionarily conserved NuA4 complex
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?
additional information
?
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HBO1 interacts both with transcriptional activator proteins and with MCM2 and ORC1
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?
additional information
?
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MYST1 specificity to Lys16 of histone H4 is not absolute, because in experiments in vitro the protein is also able to acetylate histones H3 and H2A, whereas in vivo only modification of histone H4 is specific
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?
additional information
?
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no activity with histones H3, H2A and H2B by recombinant MOF in HeLa nucleosomes
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?
additional information
?
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no activity with histones H3, H2A and H2B by recombinant MOF in HeLa nucleosomes
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?
additional information
?
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p/CAF and p300 appear to be constitutive HATs that do not require helper proteins to exhibit full catalytic activity
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?
additional information
?
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p300 performs autoacetylation, overview
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?
additional information
?
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assembly of the enzyme into male-specific lethal, MSL, or non-specific lethal, NSL, complexes controls its substrate specificity. Although MSL-associated enzyme acetylates nucleosomal histone H4 almost exclusively on lysine 16, NSL-associated enzyme exhibits a relaxed specificity and also acetylates nucleosomal histone H4 on lysines 5 and 8
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?
additional information
?
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assembly of the enzyme into male-specific lethal, MSL, or non-specific lethal, NSL, complexes controls its substrate specificity. Although MSL-associated enzyme acetylates nucleosomal histone H4 almost exclusively on lysine 16, NSL-associated enzyme exhibits a relaxed specificity and also acetylates nucleosomal histone H4 on lysines 5 and 8
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?
additional information
?
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Glu187 and Glu276 could act as the general catalytic base and together with Asp277 have a cumulative effect on deprotonation of the ?-amino group of substrate Lys12 of the histone H4 peptide, which could be mediated by water molecules
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?
additional information
?
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Glu187 and Glu276 could act as the general catalytic base and together with Asp277 have a cumulative effect on deprotonation of the ?-amino group of substrate Lys12 of the histone H4 peptide, which could be mediated by water molecules
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?
additional information
?
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Brahma is a target of enzyme Kat6B
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additional information
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Brahma is a target of enzyme Kat6B
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additional information
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enzyme p300 can directly interact with myocardin, and consequently induce the acetylation of myocardin and nucleosomal histones surrounding SRF-binding sites. Acetylation of both histone and myocardin by p300
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?
additional information
?
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GCN5 directly binds to and increases the histone H3 and H4 acetylation of the cyclin E1, cyclin D1, and E2F1 promoters
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?
additional information
?
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HBO1 exerts significant acetyltransferase activity on proteins such as ORC2, MCM2, CDC6, and Geminin in in vitro assays
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additional information
?
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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additional information
?
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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additional information
?
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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additional information
?
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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additional information
?
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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-
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additional information
?
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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-
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additional information
?
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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-
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additional information
?
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high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
-
-
-
additional information
?
-
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Both human Gcn5 and PCAF have H3 and H2B as main substrates, showing the highest in vitro affinity for H3K14
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additional information
?
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lysine acetyltransferase (KAT) activity of recombinant human ARD1/NAA10, overview. Arrest defective 1 (ARD1) is the only enzyme known so far to exhibit both N-terminal acetyltransferase (NAT) and N-terminal lysine acetyltransferase (KAT) activities. Only the monomeric rhARD1/NAA10 form, but not the oligomeric form, can acetylate lysine residues of substrate proteins. rhARD1/NAA10-mediated Hsp70 acetylation increased in a time-dependent manner
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additional information
?
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lysine acetyltransferase (KAT) activity of recombinant human ARD1/NAA10, overview. Arrest defective 1 (ARD1) is the only enzyme known so far to exhibit both N-terminal acetyltransferase (NAT) and N-terminal lysine acetyltransferase (KAT) activities. Only the monomeric rhARD1/NAA10 form, but not the oligomeric form, can acetylate lysine residues of substrate proteins. rhARD1/NAA10-mediated Hsp70 acetylation increased in a time-dependent manner
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additional information
?
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recombinant hARD1/NAA10 exhibits KAT activity, which disappears soon in vitro due to enzyme oligomerization, which results in the loss of KAT activity. While oligomeric recombinant hARD1/NAA10 loses its ability for lysine acetylation, its monomeric form clearly exhibits lysine acetylation activity in vitro. Assay optimization, under optimal conditions, hARD1/NAA10 retains its KAT activity, overview
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additional information
?
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recombinant hARD1/NAA10 exhibits KAT activity, which disappears soon in vitro due to enzyme oligomerization, which results in the loss of KAT activity. While oligomeric recombinant hARD1/NAA10 loses its ability for lysine acetylation, its monomeric form clearly exhibits lysine acetylation activity in vitro. Assay optimization, under optimal conditions, hARD1/NAA10 retains its KAT activity, overview
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additional information
?
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screening of interacting proteins for substrate identification, testing of more than four hundred proteins, KAT substrate enrichment with biotin-streptavidin pulldown and semiquantitative LC-MS/MS studies, overview. The proteins are either p300- or GCN5-unique or shared by the two KATs. 3-Azidopropionyl CoA (3AZ-CoA) is applied as a bioorthogonal surrogate of acetyl-, propionyl- and butyryl-CoA for KAT substrate identification, method overview. Comparison of the substrate profiles of p300 and GCN5, different acetyl-CoA surrogates and histone peptide H3-20 or H4-20 (the first 20 amino acids from the N-terminus of histone H3 or H4) are used as substrates. 3AZ-CoA is a sensitive and specific probe for both p300 and GCN5-T612G with comparable or even stronger activity than Ac-CoA. Substrate validations
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additional information
?
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screening of interacting proteins for substrate identification, testing of more than four hundred proteins, KAT substrate enrichment with biotin-streptavidin pulldown and semiquantitative LC-MS/MS studies, overview. The proteins are either p300- or GCN5-unique or shared by the two KATs. 3-Azidopropionyl CoA (3AZ-CoA) is applied as a bioorthogonal surrogate of acetyl-, propionyl- and butyryl-CoA for KAT substrate identification, method overview. Comparison of the substrate profiles of p300 and GCN5, different acetyl-CoA surrogates and histone peptide H3-20 or H4-20 (the first 20 amino acids from the N-terminus of histone H3 or H4) are used as substrates. 3AZ-CoA is a sensitive and specific probe for both p300 and GCN5-T612G with comparable or even stronger activity than Ac-CoA. Substrate validations
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additional information
?
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substrate site specificity, overview
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additional information
?
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substrate site specificity, overview
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additional information
?
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substrate site specificity, overview
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additional information
?
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substrate site specificity, overview
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additional information
?
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substrate site specificity, overview
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additional information
?
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substrate site specificity, overview
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additional information
?
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substrate site specificity, overview
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additional information
?
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substrate site specificity, overview
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additional information
?
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
?
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
?
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
?
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
?
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
?
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Tip60 preferentially catalyzes acetylation of histone H4
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additional information
?
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Tip60 preferentially catalyzes acetylation of histone H4
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-
-
additional information
?
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Tip60 preferentially catalyzes acetylation of histone H4
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-
additional information
?
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Tip60 preferentially catalyzes acetylation of histone H4
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-
-
additional information
?
-
Tip60 preferentially catalyzes acetylation of histone H4
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-
-
additional information
?
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Tip60 preferentially catalyzes acetylation of histone H4
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-
-
additional information
?
-
Tip60 preferentially catalyzes acetylation of histone H4
-
-
-
additional information
?
-
Tip60 preferentially catalyzes acetylation of histone H4
-
-
-
additional information
?
-
Tip60 preferentially catalyzes acetylation of histone H4
-
-
-
additional information
?
-
Tip60 preferentially catalyzes acetylation of histone H4
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-
-
additional information
?
-
-
Tip60 preferentially catalyzes acetylation of histone H4
-
-
-
additional information
?
-
-
Gcn5 and PCAF protein are transcription cofactors
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?
additional information
?
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enzyme activity is regulated by phosphorylation and interaction with other regulating protein factors
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-
?
additional information
?
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Gcn5 is a coactivator of transcription
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?
additional information
?
-
-
Gcn5 and PCAF protein are transcription cofactors
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?
additional information
?
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-
Gcn5 is a coactivator of transcription
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?
additional information
?
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Gcn5 and PCAF protein are transcription cofactors
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?
additional information
?
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the nuclear cytoplasmic O-GlcNAcase and acetyltransferase, NCOAT, is a bifunctional enzyme with both glycoside hydrolase and alkyltransferase activity and contains a zinc finger-like motif responsible for substrate recognition, via making contacts with the histone tails within nucleosomes, essential for activity, overview
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?
additional information
?
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MOZ specifically interacts and associates with transcription factors such as AML1, PU.1, p53, Runx2 and NF-kappaB, functioning as their transcriptional coactivator and cooperatively activating target gene transcription
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?
additional information
?
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ATAC2 associates with GCN5 and other proteins linked to chromatin metabolism
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?
additional information
?
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-
PCAF is present in USF1/PRMT1 complexes
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?
additional information
?
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specific role of MOZ-driven acetylation in controlling a desirable balance between proliferation and differentiation during hematopoiesis. MOZ also shows activity either as Runx1 coactivator or in the induction of leukemic transformation via transcriptional intermediary factor 2, TIF2, but is not essentially required
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?
additional information
?
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the mammalian complex corresponding to the yeast NuA4 complex contains the MYST HAT Tip60. Myc recruits the Tip60 complex to the chromatin in Rat1 wild-type cells, but not in Rat1 Myc mutant cells. Hbo1 appears to function predominantly in transcriptional repression
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?
additional information
?
-
HBO1 exerts significant acetyltransferase activity on proteins such as ORC2, MCM2, CDC6, and Geminin in in vitro assays
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-
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additional information
?
-
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specific role of MOZ-driven acetylation in controlling a desirable balance between proliferation and differentiation during hematopoiesis. MOZ also shows activity either as Runx1 coactivator or in the induction of leukemic transformation via transcriptional intermediary factor 2, TIF2, but is not essentially required
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?
additional information
?
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protein participates in var gene activation
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?
additional information
?
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protein participates in var gene activation
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additional information
?
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diaminodipropylamine and 1,3-propanediamine are no substrates
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?
additional information
?
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the enzyme modulates gene expression in liver nuclei in an epigenetic manner at high blood alcohol levels, no alteratins of MAP kinase levels, overview
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?
additional information
?
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HeLa nucleosome or core histones are no substrate for recombinant SAS complex
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?
additional information
?
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for acetylation activity of Sas2, Sas4 is absolutely required, while Sas5 stimulate
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?
additional information
?
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Gcn5 is a coactivator of transcription
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?
additional information
?
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Gcn5 and PCAF protein are transcription cofactors
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-
?
additional information
?
-
-
Gcn5 and PCAF protein are transcription cofactors
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-
?
additional information
?
-
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Gcn5 and PCAF protein are transcription cofactors
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-
?
additional information
?
-
-
Gcn5 and PCAF protein are transcription cofactors
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-
?
additional information
?
-
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enzyme activity is regulated by phosphorylation and interaction with other regulating protein factors
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?
additional information
?
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MYST-related histone acetyltransferase complex NuA4: required for cell growth, required for p53-dependent transcription activation in yeast, presumably through its Yng2 subunit, homolog of the tumor suppressor ING1. GNAT-related histone acetyltransferase complex SAGA can stimulate Gal4-VP16 activation in a manner dependent on HAT activity. D´SAGA can be recruited by several yeast activators. SAGA is targeted to promoter regions proximal to the activator binding site. Once targeted, SAGA acetylates histone h3 in the vicinity of the promoter. Targeted acetylation by SAGA stabilizes its binding and that of a targeted SWI/SNF chromatin-remodeling complex. SAGA is required for both activation of the yeast ARG1 promoter by Gcn4 activator and repression by the ArgR/Mcm1 repressor complex
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?
additional information
?
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no acetylation of adrenocorticotropin or a H3 peptide
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?
additional information
?
-
in the absence of histone acceptor, slow rates of enzyme autoacetylation and of CoA formation occur
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?
additional information
?
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Esa1 is the catalytic subunit of at least two multiprotein complexes, NuA4 and Piccolo NuA4, picNuA4
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?
additional information
?
-
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HATs perform a conserved mechanism of acetyl-transfer, where the lysine-containing substrate directly attacks enzyme-bound acetyl-CoA. The ability of HATs to form distinct multi-subunit complexes provide a means to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex
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?
additional information
?
-
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HBO1, Sas2 and Sas3 are involved in transcriptional repression enhancing Sir1-mediated epigenetic gene silencing. NuA3 and NuA4 complexes contain the MYST HATs Sas3 and Esa1, respectively. Sas2 histone acetylation of H4K16 opposed by Sir2 deacetylation of H4K16 at the euchromatin/heterochromatin interface maintains the boundary between regions of transcriptionally active and silent telomeric chromatin. Esa1 plays a role in maintaining the integrity of the DNA, rather than open chromatin structure and high-level transcriptional activity
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?
additional information
?
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in addition to Asf1, Rtt109 is also functionally linked to Rtt101, Mms1, and Mms22
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?
additional information
?
-
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Rtt109 facilitates error-free replication to prevent CAG/CTG repeat contractions. The Rtt107/Rtt101 complex is recruited to stalled replication forks in an Rtt109-dependent manner
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?
additional information
?
-
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soluble histone H4 Hat1-dependently acetylated on Lys12 is present in cells arrested at all cell cycle stages, G1, S, G2/M and also G0. Histone H3 seems to be no substrate for the HAT-B complex
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?
additional information
?
-
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Gcn5 and p300 appear to be constituitive HATs that do not require helper proteins to exhibit full catalytic activity. Esa1 and Rtt109 represent low-activity HATs that are stimulated by regulatory helper proteins, Yng2-Epl1 and Vps75/Asf1, respectively. p300/CBP exhibits the broadest protein specificity, p300 prefers histone acetylation sites with a positive charge in the -3 or +4 position. Ability of some HATs to utilize longer chain acyl-CoA, i.e. propionyl-CoA
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?
additional information
?
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histone chaperone Vps75 acts as activiating subunit. The rate-determining step of the activated complex is the transfer of the acetyl group from acetyl-CoA to the acceptor lysine residue. Vps75 stimulates catalysis more than 250fold, not by contributing a catalytic base, but by stabilizing the catalytically active conformation of enzyme Rtt109
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?
additional information
?
-
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removal of lysine residues does not substantially affect the ability of NuA4 histone actyltransferase complex to acetylate remaining sites, and insertion of an additional lysine into the substrate histone H4 tail leads to rapid quintuple-acetylation. Conversion of the native histone H2A tail to an H4-like sequence results in enhanced multi-site acetylation. NuA4's site selectivity is dictated by accessibility on the nucleosome surface, the relative proximity from the histone fold domain, and a preference for intervening glycine residues with a minimal (n + 2) spacing between lysines
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?
additional information
?
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NuA4 targets histone and nonhistone proteins
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additional information
?
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NuA4 targets histone and nonhistone proteins
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additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
-
-
-
additional information
?
-
Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
-
-
-
additional information
?
-
Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
-
-
-
additional information
?
-
Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
-
-
-
additional information
?
-
Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
-
-
-
additional information
?
-
Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
-
-
-
additional information
?
-
Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
-
-
-
additional information
?
-
Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
-
-
-
additional information
?
-
Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
-
-
-
additional information
?
-
Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
-
-
-
additional information
?
-
Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview. Hpa3 also acts as D-amino-acid N-acetyltransferase, EC 2.3.1.36
-
-
-
additional information
?
-
Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
-
-
-
additional information
?
-
Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
-
-
-
additional information
?
-
Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
-
-
-
additional information
?
-
Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
-
-
-
additional information
?
-
Nut1 is a mediator of RNA polymerase II transcription subunit 5, that also has histone acetylase activity
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
-
-
-
additional information
?
-
high-resolution mass spectrometry investigations identifies 1750 proteins as substrates of the posttranslational modification of acetylation, overview
-
-
-
additional information
?
-
Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
-
-
-
additional information
?
-
Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
-
-
-
additional information
?
-
Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
-
-
-
additional information
?
-
Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
-
-
-
additional information
?
-
Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
-
-
-
additional information
?
-
-
Rtt109 facilitates error-free replication to prevent CAG/CTG repeat contractions. The Rtt107/Rtt101 complex is recruited to stalled replication forks in an Rtt109-dependent manner
-
-
?
additional information
?
-
NuA4 targets histone and nonhistone proteins
-
-
-
additional information
?
-
substrate specificity and order of acetylation of histone H4 by Hat1, overview
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-
?
additional information
?
-
-
substrate specificity and order of acetylation of histone H4 by Hat1, overview
-
-
?
additional information
?
-
-
Mst1 interacts with a number of proteins involved in chromosome integrity and centromere function, including the methyltransferase Skb1, the recombination mediator Rad22, Sc Rad52, the chromatin assembly factor Hip1, Sc Hir1, and the Msc1 protein related to a family of histone demethylases, detailed interaction analysis, overview
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-
?
additional information
?
-
-
Gcn5 appears to be constituitive HAT that does not require helper proteins to exhibit full catalytic activity
-
-
?
additional information
?
-
-
Gcn5 appears to be constituitive HAT that does not require helper proteins to exhibit full catalytic activity
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-
?
additional information
?
-
enzyme GCN5b interacts with AP2-domain proteins, apicomplexan plant-like transcription factors, as well as a core complex that includes the co-activator ADA2-A, TFIID subunits, LEO1 polymerase-associated factor (Paf1) subunit, and RRM proteins
-
-
?
additional information
?
-
-
enzyme GCN5b interacts with AP2-domain proteins, apicomplexan plant-like transcription factors, as well as a core complex that includes the co-activator ADA2-A, TFIID subunits, LEO1 polymerase-associated factor (Paf1) subunit, and RRM proteins
-
-
?
additional information
?
-
TgGCN5b performs autoacetylation. Proteome-wide acetylome analyses of Toxoplasma tachyzoites identifies seven acetylated lysines on TgGCN5b, i.e. K811, K857, K941, K989, K997, K1002, and K1027
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-
-
additional information
?
-
-
TgGCN5b performs autoacetylation. Proteome-wide acetylome analyses of Toxoplasma tachyzoites identifies seven acetylated lysines on TgGCN5b, i.e. K811, K857, K941, K989, K997, K1002, and K1027
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4 acetyl-CoA + histone H4
4 CoA + tetraacetylhistone H4
-
-
NuA4 randomly acetylates free and nucleosomal H4, with a small preference for lysines 5, 8, and 12 over 16
-
?
acetyl-CoA + beta-site amyloid precursor protein-cleaving enzyme 1
CoA + acetylated beta-site amyloid precursor protein-cleaving enzyme 1
-
-
-
-
?
acetyl-CoA + c-Myc
CoA + acetylated c-Myc
-
acetylation by Tip60 increases c-Myc protein stability in transfected H-1299 human lung carcinoma cells
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
acetyl-CoA + histone H
CoA + acetylhistone H
-
histone acetyltransferase AtGCN5 is required to regulate the floral meristem activity through the WUS/AG pathway
-
-
?
acetyl-CoA + histone H2A
CoA + acetylhistone H2A
-
acetylation at Lys5 by Tip60
-
-
?
acetyl-CoA + histone H3
CoA + acetyl-histone H3
acetyl-CoA + histone H3
CoA + acetylhistone H3
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetyl-CoA + N-terminal L-lysyl-[beta-catenin]
CoA + H+ + N-terminal Nalpha-acetyl-lysyl-[beta-catenin]
-
-
-
ir
acetyl-CoA + N-terminal L-lysyl-[Hsp70]
CoA + H+ + N-terminal Nalpha-acetyl-L-lysyl-[Hsp70]
-
-
-
ir
acetyl-CoA + p50 protein
CoA + acetyl-p50 protein
-
acetylation of p50 by p300 independent of shear stress
-
-
?
acetyl-CoA + p53
CoA + acetyl-p53
p53 protein-acetylation of the Lys120 residue
-
-
?
acetyl-CoA + p65 protein
CoA + acetyl-p65 protein
-
acetylation of p65 by p300 during translocation into the nuclei in response to shear stress
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
acetyl-CoA + [alpha-tubulin]-L-lysine40
CoA + [alpha-tubulin]-N6-acetyl-L-lysine40
-
-
-
?
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
acetyl-CoA + [AuA]-L-lysine125
CoA + [AuA]-N6-acetyl-L-lysine125
lysine residues at positions 75 and 125 of aurora kinase A (AuA) are acetylated by ARD1, mutational analysis with AUA mutant substrates, overview
-
-
?
acetyl-CoA + [AuA]-L-lysine75
CoA + [AuA]-N6-acetyl-L-lysine75
lysine residues at positions 75 and 125 of aurora kinase A (AuA) are acetylated by ARD1, mutational analysis with AUA mutant substrates, overview
-
-
?
acetyl-CoA + [beta-catenin]-L-lysine
CoA + [beta-catenin]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
acetyl-CoA + [CDC6]-L-lysine
CoA + [CDC6]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [connexin 43]-L-lysine
CoA + [connexin 43]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
acetyl-CoA + [EGR2]-L-lysine
CoA + [EGR2]-N6-acetyl-L-lysine
acetyl-CoA + [Foxo1]-L-lysine
CoA + [Foxo1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
acetyl-CoA + [histone H2A]-L-lysine5
CoA + [histone H2A]-N6-acetyl-L-lysine5
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H2B]-L-lysine
CoA + [histone H2B]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H2B]-L-lysine12
CoA + [histone H2B]-N6-acetyl-L-lysine12
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H2B]-L-lysine15
CoA + [histone H2B]-N6-acetyl-L-lysine15
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
acetyl-CoA + [histone H3]-L-lysine18
CoA + [histone H3]-N6-acetyl-L-lysine18
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H3]-L-lysine20
CoA + [histone H3]-N6-acetyl-L-lysine20
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine23
CoA + [histone H3]-N6-acetyl-L-lysine23
acetyl-CoA + [histone H3]-L-lysine56
CoA + [histone H3]-N6-acetyl-L-lysine56
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
acetyl-CoA + [histone H4]-L-lysin16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
acetyl-CoA + [NFkappaB]-L-lysine
CoA + [NFkappaB]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [p27]-L-lysine
CoA + [p27]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
acetyl-CoA + [PGC-1alpha]-L-lysine
CoA + [PGC-1alpha]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [PGC-1]-L-lysine
CoA + [PGC-1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
acetyl-CoA + [PTEN]-L-lysine
CoA + [PTEN]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 acetylation of the oncosuppressor protein PTEN on two lysine residues (Lys125 and Lys128)
-
-
?
acetyl-CoA + [STAT3]-L-lysine
CoA + [STAT3]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
androgen receptor + acetyl-CoA
acetylated androgen receptor + CoA
-
receptor signaling in prostate cancer cells is augmented by the androgen receptor coactivator p300, which transactivates and acetylates the androgen receptor in the presence of 100 nM dihydrotestosterone, involvement of p300 in neuropeptide activation of androgen receptor signaling, overview
-
-
?
ATM kinase + acetyl-CoA
acetylated ATM kinase + CoA
-
ATM protein kinase regulates the cells response to DNA damage through the phosphorylation of proteins involved in cell-cycle checkpoints and DNA repair, suppression of Tip60 blocks the activation of ATMs kinase activity, ATM autophosphorylation e.g. at Ser1981, and prevents the ATM-dependent phosphorylation of p53 and chk2, inactivation of Tip60 sensitizes cells to ionizing radiation, overview
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
piccoloNuA4 peptide + acetyl-CoA
acetyl-piccoloNuA4 peptide + CoA
the peptide is part of the physiologic enzme complex, overview
-
-
?
promyelotic leukemia zinc finger gene + acetyl-CoA
acetylated promyelotic leukemia zinc finger gene + CoA
-
-
-
-
?
additional information
?
-
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
important role of the enzyme for chromatin modulating activity
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
most likely involved in acetylation of newly synthesized histones in cytoplasm prior to chromatin assembly
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H1 is not acetylated in vivo
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
involved in chromatin remodeling and DNA repair
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H1 is not acetylated in vivo
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
involved in chromatin remodeling and DNA repair
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
the bifunctional enzyme NCOAT, nuclear cytoplasmic O-GlcNacase and acetyltransferase, may be regulated to reduce the state of glycosylation of transcriptional activators while increasing the acetylation of histones to allow for concerted activation of eukaryotic gene transcription
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
involved in dynamic equilibrium of core histone acetylation
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
Esa1 protein is involved in cell cycle regulation
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
involved in chromatin remodeling and DNA repair
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
histone H3 is the preferred substrate
-
r
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
histone acetylation on Lys16 by Sas2
-
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
neutralization of positively charged lysine residues by acetylation lowering the affinity of histone octamers for the negatively charged DNA
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
the acetyl groups function as signals for interaction of histones with other regulatory proteins, chromatin remodeling
-
?
acetyl-CoA + histone
CoA + acetylhistone
-
-
-
r
acetyl-CoA + histone H3
CoA + acetyl-histone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetyl-histone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys9
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys9, Lys14, Lys18, Lys23, Lys27, Lys36, and Lys37
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys9
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys18
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
acetylation of Lys23
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
regulation, detailed overview. Acetylation and deacetylation events, in combination with other post-translational protein modifications, generate an NF-kappaB-signaling code and regulate NF-kappaB-dependent gene transcription in an inducer- and promoter-dependent manner, overview
-
-
r
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
CBP binds and acetylates histones at neural promoters, and regulates Corpus Callosum development. CBP binds to neuronal and glial promoters and globally promotes histone acetylation in the embryonic cortex, e.g. the beta-actin promoter, overview
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
H4R3 methylation, catalyzed by PRMT1, facilitates beta-globin transcription by regulating histone acetyltransferase binding, and histone H3 and H4 acetylation, overview
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Rtt109 association with distinct histone chaperones directs substrate selection between N-terminal lysines, H3K9, H3K23, and those within the histone fold domain, H3K56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
Rtt109 is specific for histone H3, acetylation at Lys9 and Lys56. RTT109 has functions in addition to maintaining genome stability
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation at Lys18
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys56
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
acetylation of Lys14 by tGCN5 in the consensus sequence QTARKSTGGK14APRKLASK
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
-
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
preferred substrate
-
-
?
acetyl-CoA + histone H3
CoA + acetylhistone H3
preferred substrate
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys14
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
RmtA is specific for histone H4 with Arg3 as the methylation site. Methylation of histone H4 by recombinant RmtA affects the acetylation by p300/CBP, supporting aninterrelation of histone methylation and acetylation in transcriptional regulation. Important role of the enzyme for chromatin modulating activity
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys16 by MYST1 is essential for chromatin remodeling and is used for regulation of gene expression in eukaryotes. The nucleosome is a disc-shaped octamer consisting of two heterotetramers formed by histones H3/H4 and histones H2A and H2B
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Mof is required for sex chromosome dosage compensation acting in the MSL complex, which also contains Msl1-3, Mle, and RNA, to acetylate H4K16 and to increase gene transcription from the single male X chromosome
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation of Lys5, Lys8, Lys12, and Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Hat1 is a primary enzyme for di-acetylating cytosolic histone H4 at Lys5 and Lys12 in the cytosol
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
acetylation at Lys14
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
specific acetylation of Lys16, reversible acetylation of histones play an important role in regulation of chromatin structure and function. HMOF has a role in DNA damage responseduring cell cycle progression
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
HBO1 is an H4-specific histone acetylase, and is a coactivator of the DNA replication licensing factor Cdt1. HBO1 acetylase activity is essential for DNA licensing of replication origins, where it controls H4 acetylation at the origins. H4 acetylation at origins is cell-cycle regulated, with maximal activity at the G1/S transition
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
HBO1 regulates global histone H4 acetylation
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
MSL-associated MOF acetylates nucleosomal histone H4 almost exclusively on Lys16, while NSL-associated MOF exhibits a relaxed specificity and also acetylates nucleosomal histone H4 on Lys5 and Lys8
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
MYST1 specificity to Lys16 of histone H4 is not absolute, because in experiments in vitro the protein is also able to acetylate histones H3 and H2A, whereas in vivo only modification of histone H4 is specific. Acetylation at Lys16 by MYST1 is essential for chromatin remodeling and is used for regulation of gene expression in eukaryotes. The nucleosome is a disc-shaped octamer consisting of two heterotetramers formed by histones H3/H4 and histones H2A and H2B. All human autosomes are susceptible to histone H4 acetylation by Lys16 residue and acetyltransferase MYST1
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation of Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation of Lys16
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
H4R3 methylation, catalyzed by PRMT1, facilitates beta-globin transcription by regulating histone acetyltransferase binding, and histone H3 and H4 acetylation, overview
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
Mof is solely responsible for H4K16 acetylation in mouse blastocysts. Tip60 plays essential roles in cell cycle progression in vitro
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
acetylation of histone H4 by NuA4 is required for the cellular resistance to spindle stress. The NuA4 histone acetyltransferase subunit Yaf9, is required for the cellular response to spindle stress in yeast
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
exclusively acetylates of Lys16 of histone H4, the enzyme is required for bulk of H4 lysine 16 acetylation in vivo, role of SAS complex in antagonizing the speading of Sir proteins at silent loci in Saccharomyces cerevisiae
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
the level of HAT-B-dependent acK12H4 may be very low under normal growth condition
-
-
?
acetyl-CoA + histone H4
CoA + acetylhistone H4
-
both Lys12 and Lys5 of soluble, non-chromatin-bound histone H4 are in vivo targets of acetylation for the yeast HAT-B enzyme. Lys12/Lys5-acetylated histone H4 is bound to the HAT-B complex in the soluble cell fraction. Exchange of Lys for Arg at position 12 of histone H4 do not interfere with histone H4 association with the complex, but prevented acetylation on Lys5 by the HAT-B enzyme, in vivo as well as in vitro
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [alpha-tubulin]-L-lysine
CoA + [alpha-tubulin]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [ATM]-L-lysine
CoA + [ATM]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [c-myc]-L-lysine
CoA + [c-myc]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [DNMT1]-L-lysine
CoA + [DNMT1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [E2F1]-L-lysine
CoA + [E2F1]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [EGR2]-L-lysine
CoA + [EGR2]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [EGR2]-L-lysine
CoA + [EGR2]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
essential histone-like protein HBsu contains seven acetylation sites in vivo, mutational analysis using mutants hbsK86Q, hbsK41Q, hbsK3Q, hbsK41R, and hbsK37R
-
-
?
acetyl-CoA + [HBsu]-L-lysine
CoA + [HBsu]-N6-acetyl-L-lysine
essential histone-like protein HBsu contains seven acetylation sites in vivo, mutational analysis using mutants hbsK86Q, hbsK41Q, hbsK3Q, hbsK41R, and hbsK37R
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine
CoA + [histone H3]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine14
CoA + [histone H3]-N6-acetyl-L-lysine14
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine23
CoA + [histone H3]-N6-acetyl-L-lysine23
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine23
CoA + [histone H3]-N6-acetyl-L-lysine23
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine56
CoA + [histone H3]-N6-acetyl-L-lysine56
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine56
CoA + [histone H3]-N6-acetyl-L-lysine56
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H3]-L-lysine9
CoA + [histone H3]-N6-acetyl-L-lysine9
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine
CoA + [histone H4]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine12
CoA + [histone H4]-N6-acetyl-L-lysine12
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
main substrate
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 main substrate
-
-
?
acetyl-CoA + [histone H4]-L-lysine16
CoA + [histone H4]-N6-acetyl-L-lysine16
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine5
CoA + [histone H4]-N6-acetyl-L-lysine5
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
?
acetyl-CoA + [histone H4]-L-lysine8
CoA + [histone H4]-N6-acetyl-L-lysine8
-
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [p53]-L-lysine
CoA + [p53]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
-
-
-
?
acetyl-CoA + [p53]-L-lysine120
CoA + [p53]-N6-acetyl-L-lysine120
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
-
ir
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
endogenous GCN5 and EGR2 in iNKT cells
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
endogenous GCN5 and EGR2 in iNKT cells
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
-
?
acetyl-CoA + [protein]-L-lysine
CoA + [protein]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [TIP5]-L-lysine
CoA + [TIP5]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
-
-
-
?
acetyl-CoA + [TRRAP]-L-lysine
CoA + [TRRAP]-N6-acetyl-L-lysine
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
histone acetylation is an important posttranslational modification correlated with gene activation, the HAC1 is involved in the regulation of flowering time via repression of flowering locus C, the enzyme participates in many physiological processes, including proliferation, differentiation, and apoptosis
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
-
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
phosphorylation of p300 at Ser1834 by the kinase Akt is essential for its histone acetyltransferase and transcriptional activity
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
-
-
?
histone + acetyl-CoA
acetyl-histone + CoA
-
key enzyme in post-translational modification of histones associated with transcriptionally active genes
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation of Lys9, and Lys14
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
-
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
acetylation of Lys9, and Lys14
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
regulation
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
the enzyme is involved in ethanol-induced acetylation of histone H3 in hepatocytes, potential mechanism for gene expression activation by the enzyme, overview
-
-
?
histone H3 + acetyl-CoA
acetyl-histone H3 + CoA
-
-
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
acetylation of Lys5, Lys8, and Lys12, Gcn5 and transcriptional adaptor Ada2a are involved in nucleosomal histone H4 acetylation
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
-
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
-
-
-
?
histone H4 + acetyl-CoA
acetyl-histone H4 + CoA
-
-
-
?
additional information
?
-
-
affects the inflorescence meristem and stamen development in Arabidopsis thaliana
-
-
?
additional information
?
-
-
histone acetylation and deacetylation is an epigenetic mechanism in volved in regulation of mIRNA production. GCN5 has a general repressive effect on microRNAs, miRNAs, and it targets a subset of MIRNA genes, GCN5 is required for acetylation of histone H3 lysine 14 at these loci, overview
-
-
?
additional information
?
-
isoform GCN5 is not the enzyme responsible for histone acetylation at cold-regulated genes COR promoters during cold acclimation
-
-
?
additional information
?
-
-
GCN5 directly targets HSFA3 and UVH6 and affects their H3K9 and H3K14 acetylation levels
-
-
?
additional information
?
-
-
Tip60, in complex with homologues of the mammalian Tip60 complex, exhibits functional redundancy with two other groups of genes, known as synthetic multivulva A and B genes, synMUV. Therefore, the genes encoding proteins of the Tip60 complex are termed class C synMUV genes. SynMUV A and B counteract EGF to Ras to MAPK signaling and the Tip60 complex is a chromatin-modifying complex
-
-
?
additional information
?
-
-
a homologue of Moz, zMoz, occurs in zebrafish to perform a potential Moz function in the trunk region
-
-
?
additional information
?
-
-
a homologue of Moz, zMoz, occurs in zebrafish to perform a potential Moz function in the trunk region
-
-
?
additional information
?
-
-
the enzyme plays a role in chromatin structure and gene expression regulation as a catalytic component of multiprotein complexes, some of which also contain Ada2-type transcriptional coactivators
-
-
?
additional information
?
-
-
MYST1 is a part of multiprotein complexes that accomplish functions of male X chromosome activation and thereby functions of dosage compensation in Drosophila and, in mammals, global acetylation of histone H4 K16. Functional links between MYST1 and proteins ATM and p53. Interactions between MSL1 and MYST1 within the MSL complex in Drosophila melanogaster, the compensasome includes proteins MSL1, MSL2, MSL3, MLE, MOF, a histone acetyltransferase homologous to MYST1, JIL1, and two non-coding RNA: roX1 and roX2, structure and function of the compensasome, detailed overview. Cell interactome fragments including protein homologs of hampin and MYST1, overview
-
-
?
additional information
?
-
-
histones H3 and H4 and their chaperone Asf1, including RbAp48, a regulatory subunit of Hat1 enzyme, are associated with Hat1 in the cytosol of chicken cells. Hat1 regulates integrity of cytosolic histone H3-H4 containing complex, effect of Hat1 on status for the cytosolic histones H3/H4 pre-deposition complexes with respective chaperone proteins, overview
-
-
?
additional information
?
-
-
enzyme activity is regulated by phosphorylation and interaction with other regulating protein factors
-
-
?
additional information
?
-
-
MOZ and MORF genes are rearranged by chromosome abnormalities associated with several types of leukemia
-
-
?
additional information
?
-
-
MYST-related histone acetyltransferase complex Tip60 also acts as a transcriptional coactivator in several systems including class I nuclear hormone receptors, NF-kappaB and at the superoxide dismutase gene. Tip 60 has been implicated in Alzheimer disease because it stimulates transcription when asociated with the cleaved cytoplasmic tail fragment of the amyloid-beta precursor protein
-
-
?
additional information
?
-
-
Tip60 plays a role in the control of cell-related events
-
-
?
additional information
?
-
-
acetylation of proteins by the enzyme plays a critical role in the regulation of gene expression
-
-
?
additional information
?
-
-
androgen Src kinase and PKCd kinase are involved in the regulation of p300 HAT activity via bombesin, overview
-
-
?
additional information
?
-
-
deregulated HAT activity plays a role in the development of a range of cancers
-
-
?
additional information
?
-
-
the enzyme is involved in Sp1 activation of the cyclin D1 promoter, TAF1-dependent histone acetylation facilitates transcription factor binding to the Sp1 sites, thereby activating cyclin D1 transcription and ultimately G1-to-S-phase progression, regulation, overview
-
-
?
additional information
?
-
-
the histone acetyltransferase activity of p300 is required for transcriptional repression by the promyelocytic leukemia zinc finger protein
-
-
?
additional information
?
-
ATAC2 associates with GCN5 and other proteins linked to chromatin metabolism
-
-
?
additional information
?
-
-
besides the male-specific lethal, MSL, HAT complex, MOF is also a component of the second HAT complex, designated the non-specific lethal, NSL complex, substrate specificity of the NSL complex, overview. Assembly of the MOF HAT into MSL or NSL complexes controls its substrate specificity
-
-
?
additional information
?
-
besides the male-specific lethal, MSL, HAT complex, MOF is also a component of the second HAT complex, designated the non-specific lethal, NSL complex, substrate specificity of the NSL complex, overview. Assembly of the MOF HAT into MSL or NSL complexes controls its substrate specificity
-
-
?
additional information
?
-
-
HBO1 histone acetylase is involved in DNA replication licensing and associates with replication origins, located within the HPRT1 coding sequence, specifically during the G1 phase of the cell cycle in a manner that depends on the replication licensing factor Cdt1, but is independent of the Cdt1 repressor geminin
-
-
?
additional information
?
-
-
HBO1 occurs as a component of a multiprotein complex with histone H3 and H4 acetyltransferase activity in 293 cells. The mammalian complex corresponding to the yeast NuA4 complex contains the MYST HAT Tip60
-
-
?
additional information
?
-
-
in response to DNA damage, Tip60 acetylates ATM, a DNA damage related kinase, allowing for phosphorylation of Chk2 and p53 by ATM. HATs perform a conserved mechanism of acetyl-transfer, where the lysine-containing substrate directly attacks enzyme-bound acetyl-CoA. The ability of HATs to form distinct multi-subunit complexes provide a means to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex
-
-
?
additional information
?
-
-
increase in eNOS mRNA, caused by shear stress, is completely blocked by pharmacological inhibition of p300/HAT activity with curcumin or by p300 small interfering RNA
-
-
?
additional information
?
-
mechanistically, p300 acts as a transcriptional coactivator through the direct interaction with a diverse set of transcription factors and RNA polymerase II transcription machinery
-
-
?
additional information
?
-
MYST1 is a part of multiprotein complexes that accomplish functions of male X chromosome activation and thereby functions of dosage compensation in Drosophila and, in mammals, global acetylation of histone H4 K16. Functional links between MYST1 and proteins ATM and p53. MYST1 interacts with WDR5. Cell interactome fragments including protein homologs of hampin and MYST1, overview
-
-
?
additional information
?
-
-
Tip60 is part of the evolutionarily conserved NuA4 complex
-
-
?
additional information
?
-
Brahma is a target of enzyme Kat6B
-
-
?
additional information
?
-
-
Brahma is a target of enzyme Kat6B
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-
?
additional information
?
-
-
enzyme p300 can directly interact with myocardin, and consequently induce the acetylation of myocardin and nucleosomal histones surrounding SRF-binding sites. Acetylation of both histone and myocardin by p300
-
-
?
additional information
?
-
GCN5 directly binds to and increases the histone H3 and H4 acetylation of the cyclin E1, cyclin D1, and E2F1 promoters
-
-
?
additional information
?
-
-
enzyme activity is regulated by phosphorylation and interaction with other regulating protein factors
-
-
?
additional information
?
-
-
MOZ specifically interacts and associates with transcription factors such as AML1, PU.1, p53, Runx2 and NF-kappaB, functioning as their transcriptional coactivator and cooperatively activating target gene transcription
-
-
?
additional information
?
-
-
ATAC2 associates with GCN5 and other proteins linked to chromatin metabolism
-
-
?
additional information
?
-
-
PCAF is present in USF1/PRMT1 complexes
-
-
?
additional information
?
-
-
specific role of MOZ-driven acetylation in controlling a desirable balance between proliferation and differentiation during hematopoiesis. MOZ also shows activity either as Runx1 coactivator or in the induction of leukemic transformation via transcriptional intermediary factor 2, TIF2, but is not essentially required
-
-
?
additional information
?
-
-
the mammalian complex corresponding to the yeast NuA4 complex contains the MYST HAT Tip60. Myc recruits the Tip60 complex to the chromatin in Rat1 wild-type cells, but not in Rat1 Myc mutant cells. Hbo1 appears to function predominantly in transcriptional repression
-
-
?
additional information
?
-
-
specific role of MOZ-driven acetylation in controlling a desirable balance between proliferation and differentiation during hematopoiesis. MOZ also shows activity either as Runx1 coactivator or in the induction of leukemic transformation via transcriptional intermediary factor 2, TIF2, but is not essentially required
-
-
?
additional information
?
-
-
the enzyme modulates gene expression in liver nuclei in an epigenetic manner at high blood alcohol levels, no alteratins of MAP kinase levels, overview
-
-
?
additional information
?
-
-
enzyme activity is regulated by phosphorylation and interaction with other regulating protein factors
-
-
?
additional information
?
-
-
MYST-related histone acetyltransferase complex NuA4: required for cell growth, required for p53-dependent transcription activation in yeast, presumably through its Yng2 subunit, homolog of the tumor suppressor ING1. GNAT-related histone acetyltransferase complex SAGA can stimulate Gal4-VP16 activation in a manner dependent on HAT activity. D´SAGA can be recruited by several yeast activators. SAGA is targeted to promoter regions proximal to the activator binding site. Once targeted, SAGA acetylates histone h3 in the vicinity of the promoter. Targeted acetylation by SAGA stabilizes its binding and that of a targeted SWI/SNF chromatin-remodeling complex. SAGA is required for both activation of the yeast ARG1 promoter by Gcn4 activator and repression by the ArgR/Mcm1 repressor complex
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-
?
additional information
?
-
-
Esa1 is the catalytic subunit of at least two multiprotein complexes, NuA4 and Piccolo NuA4, picNuA4
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-
?
additional information
?
-
-
HATs perform a conserved mechanism of acetyl-transfer, where the lysine-containing substrate directly attacks enzyme-bound acetyl-CoA. The ability of HATs to form distinct multi-subunit complexes provide a means to regulate HAT activity by altering substrate specificity, targeting to specific loci, enhancing acetyltransferase activity, restricting access of non-target proteins, and coordinating the multiple enzyme activities of the complex
-
-
?
additional information
?
-
-
HBO1, Sas2 and Sas3 are involved in transcriptional repression enhancing Sir1-mediated epigenetic gene silencing. NuA3 and NuA4 complexes contain the MYST HATs Sas3 and Esa1, respectively. Sas2 histone acetylation of H4K16 opposed by Sir2 deacetylation of H4K16 at the euchromatin/heterochromatin interface maintains the boundary between regions of transcriptionally active and silent telomeric chromatin. Esa1 plays a role in maintaining the integrity of the DNA, rather than open chromatin structure and high-level transcriptional activity
-
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?
additional information
?
-
-
in addition to Asf1, Rtt109 is also functionally linked to Rtt101, Mms1, and Mms22
-
-
?
additional information
?
-
-
Rtt109 facilitates error-free replication to prevent CAG/CTG repeat contractions. The Rtt107/Rtt101 complex is recruited to stalled replication forks in an Rtt109-dependent manner
-
-
?
additional information
?
-
-
soluble histone H4 Hat1-dependently acetylated on Lys12 is present in cells arrested at all cell cycle stages, G1, S, G2/M and also G0. Histone H3 seems to be no substrate for the HAT-B complex
-
-
?
additional information
?
-
NuA4 targets histone and nonhistone proteins
-
-
-
additional information
?
-
-
NuA4 targets histone and nonhistone proteins
-
-
-
additional information
?
-
-
Rtt109 facilitates error-free replication to prevent CAG/CTG repeat contractions. The Rtt107/Rtt101 complex is recruited to stalled replication forks in an Rtt109-dependent manner
-
-
?
additional information
?
-
NuA4 targets histone and nonhistone proteins
-
-
-
additional information
?
-
-
Mst1 interacts with a number of proteins involved in chromosome integrity and centromere function, including the methyltransferase Skb1, the recombination mediator Rad22, Sc Rad52, the chromatin assembly factor Hip1, Sc Hir1, and the Msc1 protein related to a family of histone demethylases, detailed interaction analysis, overview
-
-
?
additional information
?
-
enzyme GCN5b interacts with AP2-domain proteins, apicomplexan plant-like transcription factors, as well as a core complex that includes the co-activator ADA2-A, TFIID subunits, LEO1 polymerase-associated factor (Paf1) subunit, and RRM proteins
-
-
?
additional information
?
-
-
enzyme GCN5b interacts with AP2-domain proteins, apicomplexan plant-like transcription factors, as well as a core complex that includes the co-activator ADA2-A, TFIID subunits, LEO1 polymerase-associated factor (Paf1) subunit, and RRM proteins
-
-
?
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(1E,4Z,6E)-1,7-bis(3-bromo-4-hydroxyphenyl)-5-hydroxyhepta-1,4,6-trien-3-one
-
cinnamoyl-II
(1E,4Z,6E)-5-hydroxy-1,7-bis(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
-
BDMC
(1E,4Z,6E)-5-hydroxy-1-(4-hydroxy-3-methoxyphenyl)-7-(4-hydroxyphenyl)hepta-1,4,6-trien-3-one
-
DMC
(2-ethoxypropoxy)benzene
-
-
(2E)-2-(ethoxycarbonyl)heptadec-2-enoic acid
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
(2E)-2-(ethoxycarbonyl)hexadec-2-enoic acid
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
(2E)-2-acetylhexadec-2-enoic acid
-
-
(2E)-2-acetylpentadec-2-enoic acid
-
-
(2E,6E)-2,6-bis[(3,4-dihydroxyphenyl)methylidene]cyclohexan-1-one
89% residual activity at 0.1 mM
(2E,6E)-2,6-bis[(3,5-dibromo-4-hydroxyphenyl)methylidene]cyclohexan-1-one
(2E,6E)-2,6-bis[(3-bromophenyl)methylidene]cyclohexan-1-one
-
-
(2E,6E)-2,6-bis[(3-fluoro-4-hydroxyphenyl)methylidene]cyclohexan-1-one
6.3% residual activity at 0.1 mM
(2E,6E)-2,6-bis[(4-hydroxy-3,5-dimethylphenyl)methylidene]cyclohexan-1-one
-
-
(2E,6E)-2,6-bis[(4-hydroxy-3-iodophenyl)methylidene]cyclohexan-1-one
-
-
(2E,6E)-2,6-bis[(4-hydroxy-3-methylphenyl)methylidene]cyclohexan-1-one
3.0% residual activity at 0.1 mM
(2E,6E)-2,6-bis[(4-hydroxyphenyl)methylidene]cyclohexan-1-one
(2E,6E)-2,6-bis[(pyridin-3-yl)methylidene]cyclohexan-1-one
-
-
(2R)-2-[2-(4-[[(3-methyl-1-oxo-1,2-dihydrobenzo[f]quinazolin-9-yl)methyl]amino]phenyl)-2-oxoethyl]pentanedioic acid
-
(2R,3S)-4-methylidene-5-oxo-2-propyltetrahydrofuran-3-carboxylic acid
-
i.e. butyrolactone MB-3, a GCN5 inhibitor
(2S)-2-(5-[[(3-methyl-1-oxo-1,2-dihydrobenzo[f]quinazolin-9-yl)methyl]amino]-1-oxo-1,3-dihydro-2H-isoindol-2-yl)pentanedioic acid
ZINC36175770
(3-oxo-1,2-benzothiazol-2(3H)-yl)(phenyl)acetic acid
-
-
(3E,5E)-1-benzyl-3,5-bis[(3,4-dihydroxyphenyl)methylidene]piperidin-4-one
19.4% residual activity at 0.1 mM
(3E,5E)-3,5-bis[(3,4-dihydroxyphenyl)methylidene]-1-methylpiperidin-4-one
82.4% residual activity at 0.1 mM
(3E,5E)-3,5-bis[(3-bromo-4-hydroxyphenyl)methylidene]-4-oxopiperidin-1-ium
-
-
(3Z,5Z)-3,5-bis[(3-bromo-4-hydroxyphenyl)methylidene]thian-4-one
7.13% residual activity at 0.1 mM
(4-(4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl) phenyl)phosphonic acid
-
(4-(4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)phenyl)phosphonic acid
-
(4E)-2-(4-acetylphenyl)-4-[[5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl]methylidene]-5-methyl-2,4-dihydro-3H-pyrazol-3-one
-
(5E)-1-(3-chloro-4-methylphenyl)-5-[(2E)-3-(furan-2-yl)prop-2-en-1-ylidene]-2-sulfanylidenedihydropyrimidine-4,6(1H,5H)-dione
-
(E)-4-(2-(5,6-dimethylbenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
(E)-4-(2-(5-bromobenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
(E)-4-(2-(5-chlorobenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
(E)-4-(2-(6-bromobenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-2-chloro-N,N-diethylbenzenesulfonamide
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-diethyl-2-fluorobenzenesulfonamide
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-diethyl-2-methylbenzenesulfonamide
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-dimethylbenzenesulfonamide
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-(4-methoxyphenyl)benzenesulfonamide
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-(4-methylbenzyl)benzenesulfonamide
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-benzylbenzenesulfonamide
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-phenylbenzenesulfonamide
(E)-N,N-diethyl-4-(2-(5-fluorobenzo[d]thiazol-2-yl)vinyl)benzenesulfonamide
(E)-N,N-diethyl-4-(2-(5-methoxybenzo[d]thiazol-2-yl)vinyl)benzenesulfonamide
(E)-N,N-diethyl-4-(2-(5-methylbenzo[d]thiazol-2-yl)vinyl)benzenesulfonamide
(NH4)2SO4
-
competitive against both acetyl-CoA and histones
1,1'-(1,4-phenylene)bis[3-(butylsulfanyl)pyrrolidine-2,5-dione]
-
-
1,3-dibenzyl-5-[(4-hydroxy-2,6-dimethylphenyl)methylidene]-1,3-diazinane-2,4,6-trione
-
-
1,3-dibenzyl-5-[(4-hydroxyphenyl)methylidene]-1,3-diazinane-2,4,6-trione
-
-
1,7-bis(3-bromo-4-hydroxyphenyl)-1,6-heptadiene-3,5-dione
-
-
1-(2-pentylphenyl)ethan-1-ol
-
-
1-(2-pentylphenyl)ethan-1-one
-
-
1-(4-(3-nitrophenyl)thiazol-2-yl)-2-(propan-2-ylidene)hydrazine
-
1-(4-(4-chlorophenyl)thiazol-2-yl)-2-(propan-2-ylidene)hydrazine
1-(S-coenzyme A)hex-5-ene
-
-
1-(S-coenzyme A)propan-2-one
-
-
1-benzyl-3,5-bis[(E)-3-bromo-4-hydroxybenzylidene]piperidin-4-one
81.6% residual activity at 0.1 mM
10-(benzyloxy)-2,3,11-trimethoxy-6,7-dihydro-5H-isoquinolino[3,2-a][2]benzazepin-8-ium chloride
-
-
13,14 disulfoxyisogarcinol
-
LTK-19
14-isopropoxyisogarcinol
-
LTK-13
14-methoxyisogarcinol
-
LTK-14
2'-chloro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
-
2'-fluoro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
-
2'-methoxy-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
-
2,2-dimethyl-5-tetradecyl-1,3-dioxane-4,6-dione
-
-
2,2-dimethyl-5-tetradecylidene-1,3-dioxane-4,6-dione
-
-
2,3,11,12-tetramethoxy-6,7-dihydro-5H-isoquinolino[3,2-a][2]benzazepin-8-ium methanesulfonate
-
-
2,3,11-trimethoxy-10-[(4-nitrophenyl)methoxy]-6,7-dihydro-5H-isoquinolino[3,2-a][2]benzazepin-8-ium bromide
-
-
2,3-difluoro-N'-(2-fluorobenzene-1-sulfonyl)-5-(pyridin-2-yl)benzohydrazide
-
WM-1119
2,3-difluoro-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2,4-difluoro-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2,5-bis[(E)-3-bromo-4-hydroxybenzylidene]cyclopentan-1-one
41.2% residual activity at 0.1 mM
2,5-dihydroxy-3-undecylcyclohexa-2,5-diene-1,4-dione
-
2,5-diphenylisothiazol-3(2H)-one
-
-
2,6-bis(3,4-dibromobenzylidene)cyclohexan-1-one
85.1% residual activity at 0.1 mM
2,6-bis(3-bromo-4-hydroxybenzylidene)cyclohexanone
2,6-bis(3-chloro-4-hydroxybenzylidene)cyclohexan-1-one
7.7% residual activity at 0.1 mM
2,6-bis(3-chloro-5-fluoro-4-hydroxybenzylidene)cyclohexan-1-one
41.1% residual activity at 0.1 mM
2,6-bis(4-hydroxy-3-iodobenzylidene)cyclohexan-1-one
5.8% residual activity at 0.1 mM
2,6-bis[(6-hydroxy-1,1'-biphenyl-3-yl)methylene]cyclohexan-1-one
92.2% residual activity at 0.1 mM
2,6-difluoro-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-(1,3-benzothiazol-2-yl)-1,2-benzothiazol-3(2H)-one
-
-
2-(2-cyclopentylidenehydrazinyl)-4-(3-methoxyphenyl)-1,3-thiazole
-
2-(2-cyclopentylidenehydrazinyl)-4-(3-nitrophenyl)-1,3-thiazole
-
2-(2-cyclopentylidenehydrazinyl)-4-(4-fluorophenyl)-1,3-thiazole
2-(2-cyclopentylidenehydrazinyl)-4-(4-methoxyphenyl)-1,3-thiazole
-
2-(2-cyclopentylidenehydrazinyl)-4-phenyl-1,3-thiazole
-
2-(2-pyridyl)-isothiazol-3(2H)-one
-
-
2-(2-[[(1S)-3-(5-[[5-(3-carbamimidamidopropyl)-3,6-dioxopiperazin-2-yl]methyl]-2-hydroxyphenoxy)-1-carboxypropyl]amino]-2-oxoethyl)-2-hydroxybutanedioic acid
-
NK13650B
2-(3,5-difluoro-4-hydroxyphenyl)-4-((5-(4,5-dimethyl-2-(trifluoromethyl)phenyl)furan-2-yl)methylene)-5-methyl-2,4-dihydro-3H-pyrazol-3-one
-
2-(3,5-difluoro-4-hydroxyphenyl)-4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-5-methyl-2,4-dihydro-3H-pyrazol-3-one
-
2-(3,5-difluoro-4-hydroxyphenyl)-5-methyl-4-((5-(2-(trifluoromethoxy)phenyl)furan-2-yl)methylene)-2,4-dihydro-3H-pyrazol-3-one
-
2-(3,5-difluoro-4-hydroxyphenyl)-5-methyl-4-((5-(3-oxo-2,3-dihydro-1H-inden-4-yl)furan-2-yl)methylene)-2,4-dihydro-3H-pyrazol-3-one
-
2-(3-chloro-4-fluorophenyl)isothiazol-3(2H)-one
-
2-(3-fluoro-5-(2-((2-fluorophenyl)sulfonyl)hydrazinecarbonyl)-phenyl)pyridine 1-Oxide
-
2-(3-methoxyphenyl)isothiazolo[5,4-b]pyridin-3(2H)-one
-
antiproliferative effects in cancer cells, GI50 value 0.007 mM with SK-N-SH cell
2-(3-oxo-1,2-benzothiazol-2(3H)-yl)-N-(1,3-thiazol-2-yl)acetamide
-
-
2-(3-pyridyl)-isothiazol-3(2H)-one
-
-
2-(4,6-dimethyl-3-oxo[1,2]thiazolo[5,4-b]pyridin-2(3H)-yl)ethyl ethylcarbamate
-
-
2-(4-(2H-tetrazol-5-yl) phenyl)-4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-5-methyl-2,4-dihydro-3H-pyrazol-3-one
-
2-(4-(2H-tetrazol-5-yl)phenyl)-4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-5-methyl-2,4-dihydro-3H-pyrazol-3-one
-
2-(4-(trifluoromethyl)benzyl)isothiazolo[5,4-b]pyridin-3(2H)-one
-
antiproliferative effects in cancer cells, GI50 value 0.0005 mM with SK-N-SH cell, 0.030 mM with MCF-7 cell
2-(4-bromophenyl)-5-nitro[1,2]thiazolo[5,4-b]pyridin-3(2H)-one
-
2-(4-dimethylaminoaniline)-isothiazol-3(2H)-one
-
-
2-(4-fluorophenyl)isothiazolo[5,4-b]pyridin-3(2H)-one
-
antiproliferative effects in cancer cells, GI50 value 0.010 mM with SK-N-SH cell, 0.037 mM with MCF-7 cell
2-(4-fluorophenyl)[1,2]thiazolo[5,4-b]pyridin-3(2H)-one
-
PU139
2-(4-methylphenyl)isothiazolo[5,4-b]pyridin-3(2H)-one
-
antiproliferative effects in cancer cells, GI50 value 0.006 mM with SK-N-SH cell
2-(4-morpholinoaniline)-isothiazol-3(2H)-one
-
-
2-(4-pyridyl)-isothiazol-3(2H)-one
-
-
2-(4-[2-[3-(4-chlorophenyl)-5-(3,4-dimethoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4-yl]phenyl)-1H-isoindole-1,3(2H)-dione
-
-
2-(4-[2-[5-(3,4-dimethoxyphenyl)-3-(thiophen-2-yl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4-yl]phenyl)-1H-isoindole-1,3(2H)-dione
-
-
2-(4-[2-[5-(furan-2-yl)-3-(4-methoxyphenyl)-4,5-dihydro-1H-pyrazol-1-yl]-1,3-thiazol-4-yl]phenyl)-1H-isoindole-1,3(2H)-dione
-
-
2-(6,7-dihydroxynaphthyl) beta-D-xylopyranoside
-
less than 50% residual activity at 0.1 mM
2-(6,7-dimethoxynaphthyl) beta-D-xylopyranoside
-
about 80% residual activity at 0.1 mM
2-(6-fluoro-3-oxo-1,2-benzothiazol-2(3H)-yl)-N-(4-phenyl-1,3-thiazol-2-yl)acetamide
-
-
2-(6-hydroxy-7-methoxy-naphthyl) beta-D-xylopyranoside
-
less than 50% residual activity at 0.1 mM
2-(7-hydroxy-6-methoxy-naphthyl) beta-D-xylopyranoside
-
about 55% residual activity at 0.1 mM
2-(dimethylamino)-6-pentadecylpyrimidin-4(3H)-one
-
-
2-(dimethylamino)-6-tetradecylpyrimidin-4(3H)-one
-
-
2-(dimethylamino)-6-tridecylpyrimidin-4(3H)-one
-
-
2-(heptylsulfanyl)-1-(2-hydroxyphenyl)ethan-1-one
-
2-(hexylsulfanyl)-1-(2-hydroxyphenyl)ethan-1-one
-
-
2-(methylsulfanyl)-6-tridecylpyrimidin-4(3H)-one
-
-
2-(phenyl)-isothiazolo[5,4-b]pyridin-3(2H)-one
-
-
2-(S-coenzyme A)acetaldehyde
-
-
2-(S-coenzyme A)acetic acid
-
-
2-(S-coenzyme A)acetic acid thiophenyl ester
-
-
2-butyl-6-hydroxybenzoic acid
2-chloro-4-[5-[(E)-[3-[2-(4-methylanilino)-2-oxoethyl]-2,4-dioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl]benzoic acid
-
C375
2-chloro-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
-
2-cyano-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
-
2-decyl-4-hydroxyquinoline-3-carboxylic acid
-
-
2-decyl-6-hydroxybenzoic acid
88% inhibition at 0.05 mM
2-dodecylmalonate
-
compound induces hyperacetylation of specific lysine residues of histone H3, in particular residues K9 and K18, and raises the level of pan-acetylated H4. Compound inhibits the acetylation of all the other H3 and H4 lysines, with the exception of residue K8Ac of histone H4
2-ethylisothiazol-3(2H)-one
-
2-fluoro-3-hydroxy-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-3-methyl-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-4-methyl-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-5-hydroxy-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-5-methoxy-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-5-methyl-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-6-methoxy-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(2-fluoro-5-methyl-3-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(2-fluoro-5-methyl-3-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(2-phenylisonicotinoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-(4-fluoro-1H-pyrazol-1-yl)-5-methylbenzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-(4-fluoro-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-(furan-2-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-(thiophen-2-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-(thiophen-3-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-fluoro-5-(1H-pyrazol-1-yl)benzoyl)-3-methoxybenzenesulfonohydrazide
-
2-fluoro-N'-(3-fluoro-5-(1H-pyrazol-1-yl)benzoyl)-4-methoxybenzenesulfonohydrazide
-
2-fluoro-N'-(3-fluoro-5-(1H-pyrazol-1-yl)benzoyl)-5-hydroxybenzenesulfonohydrazide
-
2-fluoro-N'-(3-fluoro-5-(1H-pyrazol-1-yl)benzoyl)-5-methoxybenzenesulfonohydrazide
-
2-fluoro-N'-(3-fluoro-5-(2H-1,2,3-triazol-2-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-fluoro-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-fluoro-5-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-fluoro-5-(5-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-fluoro-5-(pyridin-2-yl)benzoyl)-3-hydroxybenzenesulfonohydrazide
-
2-fluoro-N'-(3-fluoro-5-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
competes with Ac-CoA by binding to the Ac-CoA binding site
2-fluoro-N'-(3-iodobenzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-isobutoxybenzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-isopropoxybenzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-isopropylbenzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-methoxy-5-(1H-pyrazol-1-yl)benzoyl)-benzenesulfonohydrazide
-
2-fluoro-N'-(3-methoxy-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-methoxy-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-methoxy-5-(pyrimidin-2-yl)benzoyl)-benzenesulfonohydrazide
-
2-fluoro-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-methyl-5-(2H-1,2,3-triazol-2-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-methyl-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-methyl-5-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-methyl-5-(5-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-methylbenzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-propoxybenzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(3-propylbenzoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(4-fluoro-5-methyl-[1,1'-biphenyl]-3-carbonyl)benzenesulfonohydrazide
-
2-fluoro-N'-(5-fluoro-[1,1'-biphenyl]-3-carbonyl)-3-hydroxybenzenesulfonohydrazide
-
2-fluoro-N'-(5-fluoro-[1,1'-biphenyl]-3-carbonyl)-4-hydroxybenzenesulfonohydrazide
-
2-fluoro-N'-(5-fluoro-[1,1'-biphenyl]-3-carbonyl)-4-methoxybenzenesulfonohydrazide
-
2-fluoro-N'-(5-phenylnicotinoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(6-phenylpicolinoyl)benzenesulfonohydrazide
-
2-fluoro-N'-(naphthalene-2-sulfonyl)benzohydrazide
2-fluoro-N'-(phenylsulfonyl)benzohydrazide
-
2-fluoro-N'-[(3-fluorophenyl)sulfonyl]benzohydrazide
-
2-fluoro-N'-[[3-(trifluoromethyl)phenyl]sulfonyl]benzohydrazide
-
2-hydroxy-5-nonylbenzoic acid
-
-
2-hydroxy-5-pentadecylbenzoic acid
85% inhibition at 0.05 mM
2-hydroxy-5-pentylbenzoic acid
-
2-hydroxy-5-tetradecylbenzoic acid
-
-
2-hydroxy-6-(11-hydroxyundecyl)benzoic acid
2-hydroxy-6-(5-hydroxypentyl)benzoic acid
-
2-hydroxy-6-nonylbenzoic acid
-
-
2-hydroxy-6-pentadecylbenzoic acid
2-hydroxy-6-tetradecylbenzoic acid
-
-
2-hydroxy-6-[(8E,11E)-pentadeca-8,11,14-trienyl]benzoic acid
-
2-hydroxy-6-[(E)-pentadec-8-enyl]benzoic acid
-
2-hydroxy-6-[(Z)-2-[4-(pentyloxy)phenyl]ethenyl]benzoic acid
-
-
2-hydroxy-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
-
2-pentylisothiazol-3(2H)-one
-
2-phenyl-5-(trityloxymethyl)isothiazol-3(2H)-one
-
-
2-phenylisothiazol-3(2H)-one
-
-
2-sulfanylidene-6-tridecyl-2,3-dihydropyrimidin-4(1H)-one
-
-
2-tert-butyl-5-(dodecylthio)isothiazol-3(2H)-one-1-oxide
-
-
2-tert-butyl-5-chloroisothiazol-3(2H)-one 1-oxide
-
-
2-tridecylmalonate
-
inhibition of the acetylation of histone H3 residuesK9/K18, being practically inactive in all the other assays
2-undecylmalonate
-
compound exhibits a significant inhibition of the acetylation of almost any lysine residue explored, with the sole exception of residue K8 of H4. Compound reduces the level of K5Ac of H4 and, more markedly, K16Ac of H4
2-[(1E)-1-[2-[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]ethyl]pyridine
-
2-[(1Z)-1-[(3E)-3-[2-[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]cyclopentylidene]ethyl]pyridine
-
-
2-[(3,4-dichlorophenyl)methyl]-1H-1l4-[1,2]thiazolo[5,4-b]pyridine-1,3(2H)-dione
-
-
2-[(3,4-dichlorophenyl)methyl]-1H-1l6-[1,2]thiazolo[5,4-b]pyridine-1,1,3(2H)-trione
-
-
2-[(4-bromophenyl)methyl]-5-methyl[1,2]thiazolo[5,4-b]pyridin-3(2H)-one
-
NSC694614
2-[(4-methoxyphenyl)methyl]-5-nitro[1,2]thiazolo[5,4-b]pyridin-3(2H)-one
-
NSC694622
2-[2-(4-heptylphenyl)ethyl]-6-hydroxybenzoic acid
2-[4-(4-methylphenyl)-1,3-thiazol-2-yl]-1,2-benzothiazol-3(2H)-one
-
-
2-[[4-(trifluoromethyl)phenyl]methyl][1,2]thiazolo[5,4-b]pyridin-3(2H)-one
-
PU141
3'-chloro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
-
3'-cyano-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
-
3'-fluoro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
-
3'-methoxy-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
-
3'-O-(4-benzoylbenzoyl)adenosine 5'-triphosphate
ZINC65731330
3,3'-[(2-oxocyclohexane-1,3-diylidene)di(E)methanylylidene]dibenzonitrile
-
-
3-(2-(2-fluorobenzoyl)hydrazinylsulfono)benzamide
-
3-(Z)-(benzylsulfanyl)propenoic acid
-
-
3-(Z)-(benzylsulfinyl)-2-N-(4-dimethylaminoanilino)-propenamide
-
-
3-(Z)-(benzylsulfinyl)-2-N-(4-morpholinoanilino)-propenamide
-
-
3-(Z)-(benzylsulfinyl)-N-(2-pyridyl)propenamide
-
-
3-(Z)-(benzylsulfinyl)-N-(3-pyridyl)propenamide
-
-
3-(Z)-(benzylsulfinyl)-N-(4-pyridyl)propenamide
-
-
3-amino-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
-
3-bromo-N'-(3-ethoxybenzoyl)-2-fluorobenzenesulfonohydrazide
-
3-chloro-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
-
3-chloro-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
-
3-cyano-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
-
3-fluoro-N'-(2-fluorobenzene-1-sulfonyl)-5-(1H-pyrazol-1-yl)benzohydrazide
-
3-fluoro-N'-(2-fluorobenzene-1-sulfonyl)-5-(furan-2-yl)benzohydrazide
-
3-fluoro-N'-(2-fluorobenzene-1-sulfonyl)-5-(pyrimidin-2-yl)benzohydrazide
-
3-fluoro-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
-
3-methyl-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
-
3-pentadecylidenepentane-2,4-dione
-
inhibition of the acetylation of histone H3 residuesK9/K14, being practically inactive in all the other assays
3-quinolinecarboxylic acid ethyl ester
3-Z-benzylsulfanyl-4-trityloxy-but-2-enoic acid phenylamide
-
-
3-Z-benzylsulfinyl-4-trityloxy-but-2-enoic acid phenylamide
-
-
3-[(1E)-1-[2-[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]ethyl]-2H-1-benzopyran-2-one
-
3-[(1Z)-1-[(3E)-3-[2-[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]cyclopentylidene]ethyl]-2H-1-benzopyran-2-one
-
-
3-[(E)-[2-[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]methyl]-2,3-dihydro-1H-indole
-
3-[(Z)-[(3E)-3-[2-[4-(4-chlorophenyl)-1,3-thiazol-2-yl]hydrazinylidene]cyclopentylidene]methyl]-1H-indole
-
-
3-[2-(pentadecanoylamino)benzamido]benzoic acid
-
-
3-[2-(tridecanoylamino)benzamido]benzoic acid
-
-
3-[2-[(2E)-2-(3-methylcyclopentylidene)hydrazinyl]-1,3-thiazol-4-yl]-2H-1-benzopyran-2-one
-
-
3-[2-[(2Z)-2-(3-methylcyclopentylidene)hydrazinyl]-1,3-thiazol-4-yl]-2H-1-benzopyran-2-one
-
3-[2-[2-(propan-2-ylidene)hydrazinyl]-1,3-thiazol-4-yl]-2H-1-benzopyran-2-one
-
4'-chloro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
-
4'-cyano-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
-
4'-fluoro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
-
4'-methoxy-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
-
4,4'-(2-hydroxycyclohexane-1,3-diylidene)bis(methanylylidene)-bis(2-bromophenol)
12.5% residual activity at 0.1 mM
4,5-dichloro-2-ethylisothiazol-3(2H)-one
-
-
4,5-dichloro-2-ethylisothiazol-3(2H)-one-1-oxide
-
-
4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-5-methyl-2-(4- (methylsulfonyl) phenyl)-2,4-dihydro-3H-pyrazol-3-one
-
4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-5-methyl-2-(4-(methylsulfonyl)phenyl)-2,4-dihydro-3H-pyrazol-3-one
-
4-(3-cyclopropyl-4-((5-(4,5-dimethyl-2-(trifluoromethyl)phenyl)thiophen- 2-yl)methylene)-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(3-cyclopropyl-4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(3-methyl-4-((5-(2-nitrophenyl)furan-2-yl)methylene)-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(3-methyl-5-oxo-4-((5-(2-(trifluoromethoxy)phenyl)furan-2-yl)methylene)-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(3-methyl-5-oxo-4-((5-(3-oxo-2,3-dihydro-1H-inden-4-yl)furan-2-yl)methylene)-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(3-oxo-1,2-benzothiazol-2(3H)-yl)butanoic acid
-
-
4-(4-((2-(4,5-dimethyl-2-nitrophenyl)thiazol-5-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(4-((5-(2-(difluoromethyl)phenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(4-((5-(2-(dimethylphosphoryl)phenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(4-((5-(4,5-dimethyl-2-(trifluoromethyl)phenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)-1H-pyrrol-2-yl)methylene)-3-methyl-5-oxo-4, 5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-2,5-dioxoimidazolidin-1-yl)benzoic acid
-
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-3-ethyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
C646, selective inhibitor
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzonitrile
-
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)thiophen-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(4-(1-(5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)ethylidene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(4-(2-((4,5-dimethyl-2-nitrophenyl)amino)-2-oxoethyl)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(4-(3-((4,5-dimethyl-2-nitrophenyl)amino)-3-oxopropyl)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
-
4-(4-bromophenyl)-2-[2-(propan-2-ylidene)hydrazinyl]-1,3-thiazole
4-(4-chlorophenyl)-2-(2-cyclopentylidenehydrazinyl)-1,3-thiazole
4-(4-chlorophenyl)-2-[(2E)-2-(3-cyclooctylcyclopentylidene)hydrazinyl]-1,3-thiazole
-
-
4-(4-chlorophenyl)-2-[(2E)-2-(3-methylcyclopentylidene)hydrazinyl]-1,3-thiazole
-
CPTH6
4-(4-chlorophenyl)-2-[(2E)-2-[(3Z)-3-(1-cyclohexylethylidene)cyclopentylidene]hydrazinyl]-1,3-thiazole
-
-
4-(4-chlorophenyl)-2-[(2E)-2-[(3Z)-3-(4,4-dimethylcyclohex-2-en-1-ylidene)cyclopentylidene]hydrazinyl]-1,3-thiazole
-
-
4-(4-chlorophenyl)-2-[(2E)-2-[(3Z)-3-[1-(1,3-thiazol-2-yl)ethylidene]cyclopentylidene]hydrazinyl]-1,3-thiazole
-
-
4-(4-chlorophenyl)-2-[(2E)-2-[1-(1,3-thiazol-2-yl)ethylidene]hydrazinyl]-1,3-thiazole
-
4-(4-chlorophenyl)-2-[(2E)-2-[3-(propan-2-ylidene)cyclopentylidene]hydrazinyl]-1,3-thiazole
-
-
4-(4-chlorophenyl)-2-[2-(propan-2-ylidene)hydrazinyl]-1,3-thiazole
-
4-(4-nitrophenyl)-2-[2-(propan-2-ylidene)hydrazinyl]-1,3-thiazole
-
-
4-(5-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-2,4- dioxothiazolidin-3-yl)benzoic acid
-
4-(5-(4,5-dimethyl-2-nitrobenzoyl)-1H-indazol-1-yl)benzoic acid
-
4-(5-(4,5-dimethyl-2-nitrobenzoyl)-1H-indol-1-yl)benzoic acid
-
4-(5-(4,5-dimethyl-2-nitrobenzyl)-1H-indazol-1-yl)benzoic acid
-
4-(aminoacetyl)-N-benzyl-2-methyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
4-([(2E)-2-cyano-3-[5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl]prop-2-enoyl]amino)benzoic acid
-
4-([4-[3-(methoxycarbonyl)-2,7,7-trimethyl-5-oxo-1,4,5,6,7,8-hexahydroquinolin-4-yl]phenoxy]methyl)benzoic acid
-
-
4-acetyl-2-methyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
4-acetyl-2-methyl-N-(morpholin-4-yl)-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
4-acetyl-2-methyl-N-phenyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
4-acetyl-2-methyl-N-propyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
4-acetyl-N,N-dibenzyl-2-methyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
4-acetyl-N-benzyl-2-methyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
4-acetyl-N-cyclohexyl-2-methyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
4-acetyl-N-[(3-bromophenyl)methyl]-2-methyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
4-acetyl-N-[(4-methoxyphenyl)methyl]-2-methyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
4-amino-1-naphthol
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 4A1N
4-amino-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
-
4-azidomethyl-2-phenyl-isothiazol-3(2H)-one
-
-
4-bromomethyl-2-phenylisothiazol-3(2H)-one
-
-
4-butoxy-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
-
4-chloro-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
-
4-cyano-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
-
4-hydroxy-2-methylquinoline-3-carboxylic acid
-
-
4-hydroxy-2-pentadecylquinoline-3-carboxylic acid
-
-
4-hydroxy-2-pentylquinoline-3-carboxylate
-
effects in vivo, overview, in vitro clear reduction of the acetylation extents of both histone H3 and alpha-tubulin at 0.1 mM
4-hydroxy-2-pentylquinoline-3-carboxylic acid
4-hydroxy-3-[(E)-[[2-(3-iodophenyl)-1,3-benzoxazol-5-yl]imino]methyl]benzoic acid
-
C146
4-hydroxy-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
-
4-methoxymethyl-2-phenyl-isothiazol-3(2H)-one
-
-
4-methyl-2-phenylisothiazol-3(2H)-one
-
-
4-methyl-5-methoxy-2-phenyl-isothiazol-3(2H)-one
-
-
4-trityloxy-but-2-ynoic acid phenylamide
-
-
4-[(4Z)-4-[[5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]-N-(prop-2-yn-1-yl)benzamide
i.e. C646-yne, docking study and protein interaction analysis, formation of a stable C646-cysteine adducts. The major targets of C646-yne reactivity are abundant cellular proteins containing reactive cysteine residues
4-[(4Z)-4-[[5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
i.e. C646, inhibits the lysine acetyltransferases (KATs) p300 and CBP and represents a very potent and selective small molecule KAT inhibitor, docking study and protein interaction analysis. The pyrazolone-furan of C646 is an electrophilic chemotype capable of irreversible protein reactivity
4-[2-(pentadecanoylamino)benzamido]benzoic acid
-
-
4-[2-(tridecanoylamino)benzamido]benzoic acid
-
-
4-[4-(3,4-dicarboxybenzamido)phenoxy]benzene-1,2-dicarboxylic acid
ZINC03143991
4-[4-(3,4-dimethylbenzamido)phenoxy]benzene-1,2-dicarboxylic acid
-
4-[4-(3-methylbenzamido)phenoxy]benzene-1,2-dicarboxylic acid
ZINC09694266
4-[[(4-methoxybenzene-1-sulfonyl)oxy]imino]-2,6-dimethylcyclohexa-2,5-dien-1-one
-
L002
4-[[2,6-dibromo-4-(3,3,6,6-tetramethyl-1,8-dioxo-1,2,3,4,5,6,7,8,9,10-decahydroacridin-9-yl)phenoxy]methyl]benzoic acid
-
DC-G16-11
4-[[2,6-dichloro-4-(1,8-dioxo-1,2,3,4,5,6,7,8,9,10-decahydroacridin-9-yl)phenoxy]methyl]benzoic acid
-
-
4-[[2-bromo-4-(3,3,6,6-tetramethyl-1,8-dioxo-1,2,3,4,5,6,7,8,9,10-decahydroacridin-9-yl)phenoxy]methyl]benzoic acid
-
-
4-[[4-(1,8-dioxo-1,2,3,4,5,6,7,8,9,10-decahydroacridin-9-yl)-2-methoxyphenoxy]methyl]benzoic acid
-
-
4-[[4-(3-cyano-2-methyl-5-oxo-1,4,5,6,7,8-hexahydroquinolin-4-yl)phenoxy]methyl]benzoic acid
-
-
4-[[4-(8-oxo-7,8,9,10,11,12-hexahydrobenzo[c]acridin-7-yl)phenoxy]methyl]benzoic acid
-
-
5,5'-disulfanediylbis(1,2-thiazole)
-
NU9056
5,5'-[(5-carboxy-2-oxocyclohexane-1,3-diylidene)bis(methanylylidene)]bis(2-hydroxybenzoic acid)
70.1% residual activity at 0.1 mM
5-acetoxymethyl-2-phenylisothiazol-3(2H)-one
-
-
5-azidomethyl-2-phenylisothiazol-3(2H)-one
-
-
5-bromo-2-(dimethylamino)-6-tetradecylpyrimidin-4(3H)-one
-
-
5-bromo-2-(dimethylamino)-6-tridecylpyrimidin-4(3H)-one
-
-
5-bromo-N'-(3-ethoxybenzoyl)-2-fluorobenzenesulfonohydrazide
-
5-butyl-2-hydroxybenzoic acid
-
-
5-chloro-2-(3-chloro-4-fluorophenyl)isothiazol-3(2H)-one
-
5-chloro-2-(4-nitrophenyl)-1,2-thiazol-3(2H)-one
-
CCT077791
5-chloro-2-ethyl-4-methyl-1H-1l4,2-thiazole-1,3(2H)-dione
-
-
5-chloro-2-ethyl-4-methylisothiazol-3(2H)-one
-
-
5-chloro-2-ethyl-4-methylisothiazol-3(2H)-one-1-oxide
-
-
5-chloro-2-ethylisothiazol-3(2H)-one
5-chloro-2-ethylisothiazol-3(2H)-one-1-oxide
-
-
5-chloro-2-pentylisothiazol-3(2H)-one
-
5-chloro-4-methyl-2-phenylisothiazol-3(2H)-one
-
-
5-chloro-6-[([1-[(2R)-2-hydroxy-2-(6-methoxyquinolin-4-yl)ethyl]piperidin-4-yl]amino)methyl]-1,3-benzoxazol-2(3H)-one
-
5-decyl-2-hydroxybenzoic acid
95% inhibition at 0.05 mM
5-hydroxy-2,3-dimethylnaphthalene-1,4-dione
-
PTK1
5-hydroxy-2-methylnaphthalene-1,4-dione
-
RTK1
5-hydroxymethyl-2-phenylisothiazol-3(2H)-one
-
-
5-methyl-2-phenylisothiazol-3(2H)-one
-
-
5-phenylureidomethyl-2-phenylisothiazol-3(2H)-one
-
-
6-(4-chlorophenyl)-2-(2-(3-methylcyclopentylidene)hydrazinyl)pyrimidin-4(3H)-one
-
6-(4-chlorophenyl)-2-(2-cyclopentylidenehydrazinyl)pyrimidin-4(3H)-one
-
6-(4-chlorophenyl)-2-[(2E)-2-(3-methylcyclopentylidene)hydrazinyl]pyrimidin-4(3H)-one
-
-
6-dodecyl-2-(methylsulfanyl)pyrimidin-4(3H)-one
-
-
6-dodecyl-2-sulfanylidene-2,3-dihydropyrimidin-4(1H)-one
-
-
6-[(4S)-5-(ethoxycarbonyl)-6-methyl-2-oxo-4-phenyl-3,4-dihydropyrimidin-1(2H)-yl]hexanoic acid
ZINC14246093
6-[(4S)-5-(ethoxycarbonyl)-6-methyl-2-oxo-4-[4-(trifluoromethoxy)phenyl]-3,4-dihydropyrimidin-1(2H)-yl]hexanoic acid
ZINC40152345
6-[(4S)-5-(ethoxycarbonyl)-6-methyl-4-(3-nitrophenyl)-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoic acid
-
6-[(4S)-5-[(benzyloxy)carbonyl]-4-([1,1'-biphenyl]-4-yl)-6-methyl-2-oxo-3,4-dihydropyrimidin-1(2H)-yl]hexanoic acid
ZINC08829517
8-benzyl-10,11-dimethoxy-5,6,7,9,14,14a-hexahydro-2H-[1,3]dioxolo[4,5-h]isoquinolino[3,2-a][2]benzazepin-8-ium bromide
-
-
8-benzyl-11,12-dimethoxy-5,6,7,9,14,14a-hexahydro-2H-[1,3]dioxolo[4,5-h]isoquinolino[3,2-a][2]benzazepin-8-ium bromide
-
-
8-benzyl-2,3,10,11-tetramethoxy-5,6,7,9-tetrahydroisoquinolino[3,2-a][2]benzazepin-8-ium chloride
-
-
8-benzyl-2,3,11,12-tetramethoxy-5,6,7,9-tetrahydroisoquinolino[3,2-a][2]benzazepin-8-ium bromide
-
-
9-[3-bromo-4-[(3-fluorophenyl)methoxy]phenyl]-3,4,6,7,9,10-hexahydroacridine-1,8(2H,5H)-dione
-
-
9-[4-(benzyloxy)-3-bromophenyl]-3,3,6,6-tetramethyl-3,4,6,7,9,10-hexahydroacridine-1,8(2H,5H)-dione
-
-
Ac-ARTK(me)QTARK(me)3STGGK(CoA)APRKQL
-
-
Ac-ARTK(me)QTARKSTGGK(Br)APRKQL
-
-
Ac-ARTK(me)QTARKSTGGK(CoA)APRKQL
-
-
Ac-ARTKQTARK(me)3STGGK(Sme)APRKQL
-
-
Ac-ARTKQTARKSTGGK(Br)APRKQL
-
-
Ac-ARTKQTARKSTGGK(CoA)APRKQL
-
-
Ac-L-Lys(CoA)-NH2
bisubstrate inhibitor
acetylated histone H3 peptide
-
allspice hot water extract
-
leads to a potent anti-HAT activity since the allspice hot water extract possesses a strong inhibitory effect on p300 and CBP (40% at 0.1 ng/ml). Chromatin immunoprecipitation indicates that the acetylation of histone H3 in the PSA and B2M promoter regions was also repressed
-
B-homo berberine
-
10,11-dimethoxy-6,7-dihydro-2H,5H-[1,3]dioxolo[4,5-h]isoquinolino[3,2-a][2]benzazepin-8-ium methanesulfonate
B-homo palmatine
-
2,3,10,11-tetramethoxy-6,7-dihydro-5H-isoquinolino[3,2-a][2]benzazepin-8-ium methanesulfonate
benzyl [2-(5-chloro-3-oxoisothiazol-2(3H)-yl)ethyl]carbamate
-
BF1
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
bisubstrate analogue histone H3-peptide-coenzyme A
-
bisubstrate analogue methyl-histone H3-peptide-coenzyme A
-
peptide consisting of 20 and 7 amino acid residues
-
CCT004463
-
in vivo cell proliferation inhibition
CCT004464
-
in vivo cell proliferation inhibition
CCT004465
-
in vivo cell proliferation inhibition
CCT004466
-
in vivo cell proliferation inhibition
CCT004467
-
in vivo cell proliferation inhibition
CCT077791
-
IC50: 0.0022-0.0073 mM, in vivo cell proliferation inhibition, reduces acetylation of histones H3 and H4 and alpha-tubulin in cancer cell lines
CCT077792
-
IC50: 0.0027-0.015 mM, in vivo cell proliferation inhibition
CCT077796
-
IC50: 0.0187-0.0202 mM, in vivo cell proliferation inhibition
CCT079769
-
IC50: 0.0547 mM, in vivo cell proliferation inhibition
CPTH6
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 27% inhibition at 0.1 mM; 40% inhibition at 0.8 mM; 40% inhibition at 0.8 mM
CtpB
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
-
CTX-0124143
i.e. N'-(2-fluorobenzoyl)naphthalene-2-sulfonohydrazide
Cu2+
-
5 mM, enzyme form B
DELTA12-prostaglandin J2
-
-
diethyl (1-aminotetradecyl)propanedioate
-
-
diethyl (1-chlorotetradecyl)propanedioate
-
-
diethyl (1-hydroxytetradecyl)propanedioate
-
-
diethyl (pentadecan-2-yl)propanedioate
-
-
diethyl 2-tetradecylidenemalonate
-
compound exhibits a significant inhibition of the acetylation of almost any lysine residue explored, with the sole exception of residue K8 of H4. Compound reduces the level of K5Ac of H4 and, more markedly, K16Ac of H4
diethyl benzylidenepropanedioate
-
-
diethyl decylidenepropanedioate
-
-
diethyl dodecylidenepropanedioate
-
-
diethyl dodecylpropanedioate
-
-
diethyl pentadecylidenepropanedioate
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 i.e. SPV106, a long-chain alkylidenemalonate (LoCAM), 74% inhibition at 0.05 mM
diethyl tetradecylidenepropanedioate
-
-
diethyl tetradecylpropanedioate
-
-
diethyl tridecylidenepropanedioate
-
-
diethyl tridecylpropanedioate
-
-
diethyl undecylidenepropanedioate
-
-
diethyl [(dodecylamino)methylidene]propanedioate
-
-
diethyl [(naphthalen-1-yl)methylidene]propanedioate
-
-
diethyl [(naphthalen-2-yl)methylidene]propanedioate
-
-
dimethyl sulfoxide
-
irreversible at 2% v/v
dithiothreitol
-
10 mM: stimulation, 100 mM: inhibition
embelin
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
EML425
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
epigallocatechin-3-gallate
ethanol
-
irreversible at 2% v/v
ethyl (2E)-2-acetylheptadec-2-enoate
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
ethyl (2E)-2-acetylhexadec-2-enoate
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
ethyl (3E,5E)-3,5-bis[(3-bromo-4-hydroxyphenyl)methylidene]-4-oxocyclohexane-1-carboxylate
-
-
ethyl 2-decyl-4-hydroxyquinoline-3-carboxylate
-
-
ethyl 2-methyl-6-([5-[(prop-2-yn-1-yl)amino]pentyl]oxy)quinoline-3-carboxylate
ethyl 2-methylquinoline-3-carboxylate
ethyl 3-(5-chloro-3-oxoisothiazol-2(3H)-yl)propanoate
-
ethyl 4-hydroxy-2-methylquinoline-3-carboxylate
-
-
ethyl 4-hydroxy-2-pentadecylquinoline-3-carboxylate
-
-
ethyl 4-hydroxy-2-pentylquinoline-3-carboxylate
-
-
ethyl 4-oxo-2-sulfanylidene-6-tetradecyl-1,2,3,4-tetrahydropyrimidine-5-carboxylate
-
-
ethyl quinoline-3-carboxylate
-
MC1752
gamma-butyrolactone
-
MB-3
geminin
-
a Cdt1 repressor, inhibits HBO1 acetylase activity in a a Cdt1-dependent manner in the context of a Cdt1-HBO1 complex, and it associates with origins and inhibits H4 acetylation and licensing in vivo, but geminin does not block the interaction of Cdt1 with HBO1 in vitro or Cdt1-dependent recruitment of HBO1 to replication origins in vivo
-
H3-CoA-20-Tat
-
IC50: 0.012 mM, recombinant enzyme
-
HC toxin
cyclic tetrapeptide, decreases enzyme form B expression
heparan sulfate proteoglycans
-
heparan sulfate proteoglycans isolated from corneal and pulmonary fibroblasts inhibit HAT activity with similar effectiveness as heparin
-
heparin
-
ability of heparin to inhibit HAT is dependent upon its size and structure: small heparin-derived oligosaccharides (above 8 sugars) and N-desulfated or O-desulfated heparin show reduced inhibitory activity. Heparin is shown to bind to pCAF. Enzyme assays indicate that heparin shows the characteristics of a competitive-like inhibitor causing a 50fold increase in the Km of pCAF for histone H4
histone H3-peptide mutant K14A
-
dead-end inhibitor analogue, mutant histone H3 -peptide consisting of amino acid residues 3-20 K14A
-
Isopropanol
-
irreversible at 2% v/v
L002
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 i.e. NSC764414
LTK-14
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
Lys-CoA-Tat
-
IC50: 250 nM, recombinant enzyme, complete inhibition of acetylation of the promyelotic leukemia zinc finger gene
MC1626
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
MC1752
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
MC1823
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
methyl 2-(5-chloro-3-oxoisothiazol-2(3H)-yl)ethanoate
-
methyl 3-(3-oxoisothiazol-2(3H)-yl)propanoate
-
methyl 3-(4,5-dichloro-1-oxido-3-oxoisothiazol-2(3H)-yl)propanoate
-
-
methyl 3-(4,5-dichloro-3-oxoisothiazol-2(3H)-yl)propanoate
-
-
methyl 3-(5-chloro-1,3-dioxo-1,3-dihydro-2H-1l4,2-thiazol-2-yl)propanoate
-
-
methyl 3-(5-chloro-1-oxido-3-oxoisothiazol-2(3H)-yl)propanoate
methyl 3-(5-chloro-3-oxo-1,2-thiazol-2(3H)-yl)propanoate
-
-
methyl 3-(5-chloro-3-oxoisothiazol-2(3H)-yl)propanoate
-
-
methyl 3-(5-chloro-3-oxoisothiazol-2(3H)-yl)propanoic acid
-
methyl 3-(5-chloro-4-methyl-1,3-dioxo-1,3-dihydro-2H-1l4,2-thiazol-2-yl)propanoate
-
-
methyl 3-(5-chloro-4-methyl-1-oxido-3-oxoisothiazol-2(3H)-yl)propanoate
-
-
methyl 3-(5-chloro-4-methyl-3-oxoisothiazol-2(3H)-yl)propanoate
-
-
methyl 3-[(5-chloro-1,2-thiazol-3-yl)amino]propanoate
-
-
methyl 3-[(5-chloroisothiazol-3-yl)amino]propanoate
-
methyl 3-[4-chloro-5-(dodecylthio)-1-oxido-3-oxoisothiazol-2(3H)-yl]propanoate
-
-
methyl 3-[4-[[(benzyloxy)carbonyl]amino]-5-chloro-3-oxo-1,2-thiazol-2(3H)-yl]propanoate
-
-
methyl 3-[4-{[(benzyloxy)carbonyl]amino}-5-chloro-3-oxoisothiazol-2(3H)-yl]propanoate
-
methyl 3-[5-(dodecylthio)-1-oxido-3-oxoisothiazol-2(3H)-yl] propanoate
-
-
methyl 4-(3-oxoisothiazol-2(3H)-yl)butanoate
-
methyl 4-(5-chloro-3-oxoisothiazol-2(3H)-yl)butanoate
-
methyl 5-(5-chloro-3-oxoisothiazol-2(3H)-yl)pentanoate
-
methyl 6-(5-chloro-3-oxoisothiazol-2(3H)-yl)hexanoate
-
montelukast
-
decreases HAT activity by attenuating the activating effect of TNF-alpha
N'-( 2-fluoro-[1,1'- biphenyl]-3-carbonyl)-benzenesulfonohydrazide
-
N'-(2,3-difluorobenzoyl)benzenesulfonohydrazide
-
N'-(2,3-difluorobenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(2,6-difluorobenzene-1-sulfonyl)-3-fluoro-5-propoxybenzohydrazide
-
N'-(2,6-difluorobenzene-1-sulfonyl)-3-fluoro-5-[(propan-2-yl)oxy]benzohydrazide
-
N'-(2,6-difluorobenzene-1-sulfonyl)-3-methoxy-5-[(propan-2-yl)oxy]benzohydrazide
-
N'-(2,6-difluorobenzene-1-sulfonyl)-3-methyl-5-[(propan-2-yl)oxy]benzohydrazide
-
N'-(2-dluorobenzoyl)-4-methylbenzenesulfonohydrazide
-
N'-(2-fluoro-3-(trifluoromethyl)benzoyl)-benzenesulfonohydrazide
-
N'-(2-fluoro-3-(trifluoromethyl)benzoyl)naphthalene-2-sulfonohydrazide
-
N'-(2-fluoro-3-methoxybenzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-3-methyl-5-((2-methylallyl)oxy)benzoyl)-benzenesulfonohydrazide
-
N'-(2-fluoro-3-methyl-5-((2-methylallyl)oxy)benzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-3-methyl-5-(2H-1,2,3-triazol-2-yl)benzoyl)-naphthalene-2-sulfonohydrazide
-
N'-(2-fluoro-3-methyl-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)-benzenesulfonohydrazide
-
N'-(2-fluoro-3-methyl-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-3-methyl-5-(4-methyl-1H-pyrazol-1-yl)benzoyl)-benzenesulfonohydrazide
-
N'-(2-fluoro-3-methyl-5-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-3-methyl-5-(5-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-3-methylbenzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-3-methylbenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(2-fluoro-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-5-(2H-1,2,3-triazol-2-yl)benzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-5-(4-fluoro-1H-pyrazol-1-yl)-3-methylbenzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-5-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-5-(furan-2-yl)-3-methylbenzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-5-(furan-2-yl)benzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-5-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-5-isopropoxy-3-methylbenzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-5-isopropoxybenzoyl)benzenesulfonohydrazide
-
N'-(2-fluoro-5-methylbenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(2-fluoro-5-propoxybenzoyl)benzenesulfonohydrazide
-
N'-(2-fluorobenzene-1-sulfonyl)-3-(furan-2-yl)-5-methoxybenzohydrazide
-
N'-(2-fluorobenzene-1-sulfonyl)-3-(furan-2-yl)-5-methylbenzohydrazide
-
N'-(2-fluorobenzene-1-sulfonyl)-3-(naphthalen-2-yl)benzohydrazide
-
N'-(2-fluorobenzene-1-sulfonyl)-3-(pyrimidin-2-yl)benzohydrazide
-
N'-(2-fluorobenzene-1-sulfonyl)-3-(pyrimidin-4-yl)benzohydrazide
-
N'-(2-fluorobenzene-1-sulfonyl)-3-(trifluoromethoxy)benzohydrazide
-
N'-(2-fluorobenzene-1-sulfonyl)-3-methoxy-5-(pyridin-2-yl)benzohydrazide
-
N'-(2-fluorobenzene-1-sulfonyl)-3-methyl-5-(pyridin-2-yl)benzohydrazide
-
N'-(2-fluorobenzene-1-sulfonyl)-3-methyl-5-(pyrimidin-2-yl)benzohydrazide
-
N'-(2-fluorobenzene-1-sulfonyl)benzohydrazide
-
N'-(2-fluorobenzoyl)-2-methoxybenzenesulfonohydrazide
-
N'-(2-fluorobenzoyl)-2-methylbenzenesulfonohydrazide
-
N'-(2-fluorobenzoyl)-3-methoxybenzenesulfonohydrazide
-
N'-(2-fluorobenzoyl)-3-methylbenzenesulfonohydrazide
-
N'-(2-fluorobenzoyl)-4-methoxybenzenesulfonohydrazide
-
N'-(2-methoxybenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(2-methylbenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(2-phenylisonicotinoyl)benzenesulfonohydrazide
-
N'-(3-(1,2,4-oxadiazol-3-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(1,3,4-oxadiazol-2-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(1H-pyrazol-1-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
N'-(3-(3,5-dimethyl-1H-pyrazol-1-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(4-fluoro-1H-pyrazol-1-yl)-5-methylbenzoyl)benzenesulfonohydrazide
-
N'-(3-(allyloxy)-5-fluorobenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(allyloxy)-5-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(allyloxy)benzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(cyclopentyloxy)benzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(cyclopentyloxy)benzoyl)benzenesulfonohydrazide
-
N'-(3-(cyclopropylmethoxy)-5-fluorobenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(cyclopropylmethoxy)-5-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(cyclopropylmethoxy)benzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(ethoxymethyl)-5-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-(furan-2-yl)-5-methoxybenzoyl)benzenesulfonohydrazide
-
N'-(3-(furan-2-yl)-5-methylbenzoyl)benzenesulfonohydrazide
-
N'-(3-(piperazin-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(pyridin-3-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(pyrimidin-2-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(pyrimidin-5-yl)benzoyl)benzenesulfonohydrazide
N'-(3-(thiazol-2-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(thiazol-4-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(thiophen-2-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(thiophen-3-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(trifluoromethoxy)benzoyl)benzenesulfonohydrazide
-
N'-(3-(trifluoromethoxy)benzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-(trifluoromethyl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(trifluoromethyl)benzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-acetylbenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-aminobenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-bromobenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-butoxybenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-butoxybenzoyl)benzenesulfonohydrazide
-
N'-(3-chloro-2-fluorobenzoyl)benzenesulfonohydrazide
-
N'-(3-chloro-2-fluorobenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-chloro-5-(furan-2-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-chloro-5-(furan-2-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-chloro-5-(thiophen-2-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-cyanobenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-cyclopropoxy-5-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-ethoxy-5-fluorobenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-ethoxy-5-methoxybenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-ethoxy-5-methylbenzoyl)-2,3-difluorobenzenesulfonohydrazide
-
N'-(3-ethoxy-5-methylbenzoyl)-2,4-difluorobenzenesulfonohydrazide
-
N'-(3-ethoxy-5-methylbenzoyl)-2,5-difluorobenzenesulfonohydrazide
-
N'-(3-ethoxy-5-methylbenzoyl)-2,6-difluorobenzenesulfonohydrazide
-
N'-(3-ethoxy-5-methylbenzoyl)-2-fluoro-3-methylbenzenesulfonohydrazide
-
N'-(3-ethoxy-5-methylbenzoyl)-2-fluoro-4-methylbenzenesulfonohydrazide
-
N'-(3-ethoxy-5-methylbenzoyl)-2-fluoro-5-methylbenzenesulfonohydrazide
-
N'-(3-ethoxy-5-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-ethoxybenzoyl)-2-fluoro-5-methoxybenzenesulfonohydrazide
-
N'-(3-ethoxybenzoyl)-2-fluoro-6-methoxybenzenesulfonohydrazide
-
N'-(3-ethoxybenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-ethoxybenzoyl)benzenesulfonohydrazide
-
N'-(3-ethoxybenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-ethyl-2-fluorobenzoyl)benzenesulfonohydrazide
-
N'-(3-ethyl-2-fluorobenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-ethylbenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(3-ethylbenzoyl)benzenesulfonohydrazide
-
N'-(3-fluoro-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-fluoro-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-fluoro-5-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-fluoro-5-(furan-2-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-fluoro-5-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-fluoro-5-propoxybenzoyl)benzenesulfonohydrazide
-
N'-(3-fluorobenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-isobutoxybenzoyl)benzenesulfonohydrazide
-
N'-(3-isopropoxybenzoyl)benzenesulfonohydrazide
-
N'-(3-isopropylbenzoyl)benzenesulfonohydrazide
-
N'-(3-isopropylbenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-methoxy-5-(1H-pyrazol-1-yl)benzoyl)-benzenesulfonohydrazide
-
N'-(3-methoxy-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-methoxy-5-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-methoxybenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-methoxylbenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-methylbenzoyl)benzenesulfonohydrazide
-
N'-(3-phenoxybenzoyl)benzenesulfonohydrazide
-
N'-(3-propoxybenzoyl)benzenesulfonohydrazide
-
N'-(3-propoxybenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(3-propylbenzoyl)benzenesulfonohydrazide
-
N'-(4-(trifluoromethoxy)benzoyl)naphthalene-2-sulfonohydrazide
-
N'-(4-cyanobenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(4-fluoro-5-methyl-[1,1'-biphenyl]-3-carbonyl)-benzenesulfonohydrazide
-
N'-(4-fluoro-[1,1'-biphenyl]-3-carbonyl)-benzenesulfonohydrazide
-
N'-(4-fluorobenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(4-methoxybenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(4-methylbenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(5-(allyloxy)-2-fluoro-3-methylbenzoyl)-benzenesulfonohydrazide
-
N'-(5-(allyloxy)-2-fluoro-3-methylbenzoyl)benzenesulfonohydrazide
-
N'-(5-(allyloxy)-2-fluorobenzoyl)benzenesulfonohydrazide
-
N'-(5-(cyclopropylmethoxy)-2-fluoro-3-methylbenzoyl)-benzenesulfonohydrazide
-
N'-(5-(cyclopropylmethoxy)-2-fluoro-3-methylbenzoyl)benzenesulfonohydrazide
-
N'-(5-(ethoxymethyl)-2-fluoro-3-methylbenzoyl)-benzenesulfonohydrazide
-
N'-(5-(ethoxymethyl)-2-fluoro-3-methylbenzoyl)benzenesulfonohydrazide
-
N'-(5-chloro-4-fluoro-[1,1'-biphenyl]-3-carbonyl)-benzenesulfonohydrazide
-
N'-(5-ethoxy-2-fluoro-3-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
-
N'-(5-ethoxy-2-fluoro-3-methylbenzoyl)naphthalene-2-sulfonohydrazide
-
N'-(5-ethoxy-2-fluorobenzoyl)benzenesulfonohydrazide
-
N'-(5-phenylnicotinoyl)benzenesulfonohydrazide
-
N'-(6-phenylpicolinoyl)benzenesulfonohydrazide
-
N'-(benzenesulfonyl)-2-fluoro-3-methyl-5-(pyridin-2-yl)benzohydrazide
-
N'-(benzenesulfonyl)-2-fluoro-3-methyl-5-(pyrimidin-2-yl)benzohydrazide
-
N'-(benzenesulfonyl)-2-fluoro-3-methyl-5-[(propan-2-yl)oxy]benzohydrazide
-
N'-(benzenesulfonyl)-2-fluoro-5-(pyridazin-4-yl)benzohydrazide
-
WM-2474
N'-(benzenesulfonyl)-2-fluoro-5-(pyrimidin-2-yl)benzohydrazide
-
N'-(benzenesulfonyl)-2-fluoro-5-(pyrimidin-4-yl)benzohydrazide
-
N'-(benzenesulfonyl)-2-fluoro-5-[(prop-2-yn-1-yl)oxy]benzohydrazide
-
N'-(benzenesulfonyl)-3-fluoro-5-(pyrimidin-2-yl)benzohydrazide
-
N'-(benzenesulfonyl)-3-fluorobenzohydrazide
-
N'-(benzenesulfonyl)-3-methoxy-5-(pyrimidin-2-yl)benzohydrazide
-
N'-(benzenesulfonyl)-3-methoxybenzohydrazide
-
N'-(benzenesulfonyl)-3-methyl-5-(pyrimidin-2-yl)benzohydrazide
-
N'-(benzenesulfonyl)-4-fluoro-5-methyl[1,1'-biphenyl]-3-carbohydrazide
N'-(benzenesulfonyl)-5-chloro-4-fluoro[1,1'-biphenyl]-3-carbohydrazide
-
N'-(ethoxy-2-fluoro-3-methylbenzoyl)-benzenesulfonohydrazide
-
N'-(ethoxy-2-fluoro-3-methylbenzoyl)benzenesulfonohydrazide
-
N'-(naphthalen-2-ylsulfonyl)benzohydrazide
-
N'-(naphthalene-2-sulfonyl)benzohydrazide
-
N'-([1,1'-biphenyl]-3-carbonyl)-2-fluorobenzenesulfonohydrazide
-
N'-([1,1'-biphenyl]-3-carbonyl)benzenesulfonohydrazide
-
N'-([1,1'-biphenyl]-3-carbonyl)naphthalene-2-sulfonohydrazide
-
N'-benzoylbenzenesulfonohydrazide
-
N'-[(3-bromophenyl)sulfonyl]-2-fluorobenzohydrazide
-
N'-[(3-ethylphenyl)sulfonyl]-2-fluorobenzohydrazide
-
N'-[(4-bromophenyl)sulfonyl]-2-fluorobenzohydrazide
-
N-(2-fluoro-3-methyl-5-(2H-1,2,3-triazol-2-yl)benzoyl)benzenesulfonohydrazide
-
N-(2-fluoro-3-methyl-5-propoxybenzoyl)-benzenesulfonohydrazide
-
N-(2-fluoro-3-methyl-5-propoxybenzoyl)benzenesulfonohydrazide
-
N-(2-fluoro-4-[[(1-hydroxy-3-methylbenzo[f]quinazolin-9-yl)methyl]amino]benzoyl)-L-glutamic acid
-
N-(3-aminopropyl)acetamido-CoA
-
-
N-(3-benzamidobutyl)acetamido-CoA
-
-
N-(3-benzamidopentyl)acetamido-CoA
-
-
N-(3-benzamidopropyl)acetamido-CoA
-
-
N-(3-[[(2,2-dimethylpropanoyl)oxy]amino]propyl)acetamido-CoA
-
-
N-(4-acetyl-2-methyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonyl)benzamide
-
-
N-(4-chloro-3-trifluoromethyl-phenyl)-2-ethoxy-6-pentadecyl-benzamide
-
-
N-(4-chlorophenyl)-2-(4,6-dimethyl-3-oxo[1,2]thiazolo[5,4-b]pyridin-2(3H)-yl)acetamide
-
-
N-(4-cyano-3-(trifluoromethyl)phenyl)-2-decyl-6-ethoxybenzamide
-
inhibits human p300 recombinant enzyme similar to anacardic acid
N-(4-cyano-3-(trifluoromethyl)phenyl)-2-ethoxy-6-octylbenzamide
-
inhibits human p300 recombinant enzyme similar to anacardic acid, moreover this inhibitor induces significant apoptosis at 0.05 nM in U937 leukemia cells
N-(4-[[(1-hydroxy-3-methylbenzo[f]quinazolin-9-yl)methyl]amino]cyclohexane-1-carbonyl)-L-glutamic acid
-
N-(4-[[(2,2-dimethylpropanoyl)oxy]amino]butyl)acetamido-CoA
-
-
N-(4-[[(2-amino-4-hydroxyquinazolin-6-yl)methyl](formyl)amino]benzoyl)-L-glutamic acid
-
N-(4-[[(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)methyl](cyanomethyl)amino]benzoyl)-L-glutamic acid
ZINC29250560
N-(4-[[(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)methyl](prop-2-yn-1-yl)amino]benzoyl)-L-glutamic acid
N-(4-[[(2-amino-7-methyl-4-oxo-3,4-dihydroquinazolin-6-yl)methyl](prop-2-yn-1-yl)amino]benzoyl)-L-glutamic acid
-
N-(4-[[4-(2-amino-6-oxo-1,6-dihydropyrimidin-5-yl)benzene-1-sulfonyl]amino]benzoyl)-L-glutamic acid
-
N-(5-[[(2,2-dimethylpropanoyl)oxy]amino]pentyl)acetamido-CoA
-
-
N-benzyl-2,4-dimethyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
N-benzyl-2-methyl-4-(phenylacetyl)-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
N-benzyl-4-(chloroacetyl)-2-methyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
N-benzyl-4-(cyclohexanecarbonyl)-2-methyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
N-benzyl-4-(cyclopropanecarbonyl)-2-methyl-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
N-benzylacetamido-CoA
-
-
N-[(1S)-1-cyclopropyl-2,2,2-trifluoroethyl]-N-[(4-fluorophenyl)methyl]-2-[(1R)-5-[(methylcarbamoyl)amino]-2',4'-dioxo-2,3-dihydrospiro[indene-1,5'-[1,3]oxazolidin]-3'-yl]acetamide
-
-
N-[(2-chloro-6-fluorophenyl)methyl]-2-(2,5-dioxo-4-phenyl-4-propylimidazolidin-1-yl)-N-methylacetamide
-
-
N-[(3S)-5-[[(1S)-3-(5-[[(5S)-5-(3-carbamimidamidopropyl)-3,6-dioxopiperazin-2-yl]methyl]-2-hydroxyphenoxy)-1-carboxypropyl]amino]-3-carboxy-3-hydroxy-5-oxopentanoyl]-L-aspartic acid
-
NK13650A
N-[(4-fluorophenyl)methyl]-2-[(1R)-5-[(methylcarbamoyl)amino]-2',4'-dioxo-2,3-dihydrospiro[indene-1,5'-[1,3]oxazolidin]-3'-yl]-N-[(2S)-1,1,1-trifluoropropan-2-yl]acetamide
N-[2-(2,5-dimethoxybenzoyl)-3-methyl-1-benzofuran-6-yl]-3,5-dimethoxybenzamide
-
F2209-0381
N-[2-(S-Coenzyme A)acetyl]spermidine amide
-
strong
N-[4-([[(6S)-2-amino-5-methyl-4-oxo-3,4,5,6,7,8-hexahydropteridin-6-yl]methyl]amino)benzoyl]-L-glutamic acid
ZINC34633488
N-[4-chloro-3-(trifluoromethyl)phenyl]-2-ethoxy-6-tetradecylbenzamide
-
-
N-[4-cyano-3-(trifluoromethyl)phenyl]-2-ethoxy-6-heptylbenzamide
-
-
N-[4-[(2-methyl-4-oxo-3,4-dihydroquinazoline-6-sulfonyl)amino]benzoyl]-L-glutamic acid
-
N-[5-[(5-[[5-([4-[(5-[[5-([5-[(5-[[3-(dimethylamino)propyl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)amino]-4-oxobutyl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]-4-[(N-[[2-(2-[4-[(4Z)-4-[[5-(2,3-dimethyl-6-nitrophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzamido]ethoxy)ethoxy]acetyl]-beta-alanyl)amino]-1-methyl-1H-pyrrole-2-carboxamide
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
N6-Acetyllysine
-
competitive
NK13650A
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
NK13650B
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
peptide conjugate Boc-C5-CoA
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 peptide Boc-C5-CoA, the molecule exploits an additional electron-rich pocket (P2) about 10 A away from the lysine binding pocket (P1). Boc-C5-CoA that shows high affinity for, comprises a CoA moiety which binds to the P1 pocket, a 1,5-pentanediamine linker and a tert-butoxycarbonyl cap, which is accommodated by the P2 pocket. CoA is connected to the N1 of the linker through a carboxymethylene bridge, while the tert-butoxycarbonyl cap protects the N5
-
peptide conjugate H3-CoA-20
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 peptide H3-CoA-20 resembles the K14-containing sequence of histone H3, the main substrate of PCAF, R1 is A-P-R-K-Q-L-OH and R2 is G-G-T-S-L-R-A-T-Q-K-T-R-A-NHCH3
-
peptide conjugate H4-K16-CoA
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 peptide H4-K16-CoA, R1 is K-A-G-G-K-G-L-G-K-G-G-K-G-R-G-S-OCH3 and R2 is R-H-R-K-NH2; peptide H4-K16-CoA, R1 is K-A-G-G-K-G-L-G-K-G-G-K-G-R-G-S-OCH3 and R2 is R-H-R-K-NH2
-
phenylpyrazolocurcumin CTK7A
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
potassium phosphate
-
90 mM
PU139
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
S-(4-benzylpiperazin-1-yl)(1-oxo)ethyl-CoA
-
-
S-(piperazin-1-yl)(1-oxo)ethyl-CoA
-
-
S-(tert-butyl 4-acetylpiperazin-1-yl)(1-oxo)ethyl-CoA
-
-
Sea urchin sperm chromatin
-
-
-
siRNA
-
silencing of enzyme gene
-
sodium 4-[3,5-bis[(E)-2-(4-hydroxy-3-methoxyphenyl)ethenyl]-1H-pyrazol-1-yl]benzoate
-
CTK7A
Spd(N1)-CoA
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 obtained by linking the polyamine spermidine to CoA using a carboxymethylene bridge
spermidine
-
inhibits histone acetylation at high concentrations, enzyme forms A and B
tert-butyl-(3-(2-(naphthalen-2-ylsulfono)hydrazinecarbonyl)-phenyl)carbamate
-
tetradecylidenepropanedioic acid
-
EML264
TH1834
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 60% inhibition at 0.5 mM
tridecylidenepropanedioic acid
-
-
TTK21
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
WM-8014
highly potent inhibitor, competitive inhibition with respect to acetyl-CoA
[(3,7-dimethyloctyl)oxy]benzene
-
-
[5-(4-[[(2-phenylethyl)(4-[4-[(pyrrolidin-1-yl)methyl]phenoxy]butyl)amino]methyl]phenyl)-2H-tetrazol-2-yl]acetic acid
-
TH1834
[histone H4]-L-lysine12-CoA
bisubstrate inhibitor, i.e. Ac-SGRGKGGKGLGK(CoA)GGAKRHRK, competitive inhibition with respect to both acetyl-CoA and histone H4, highly specific inhibitor for histone acetyltransferase 1
-
[histone H4]-L-lysine16-CoA
-
[histone H4]-L-lysine5-CoA
bisubstrate inhibitor, i.e. Ac-SGRGK(CoA)GGKGLGKGGAKRHRK
-
[histone H4]-L-lysine8-CoA
bisubstrate inhibitor, i.e. Ac-SGRGKGGK(CoA)GLGKGGAKRHRK
-
(2E,6E)-2,6-bis[(3,5-dibromo-4-hydroxyphenyl)methylidene]cyclohexan-1-one
complete inhibition at 0.1 mM
(2E,6E)-2,6-bis[(3,5-dibromo-4-hydroxyphenyl)methylidene]cyclohexan-1-one
-
-
(2E,6E)-2,6-bis[(4-hydroxyphenyl)methylidene]cyclohexan-1-one
28.6% residual activity at 0.1 mM
(2E,6E)-2,6-bis[(4-hydroxyphenyl)methylidene]cyclohexan-1-one
-
-
(E)-4-(2-(5,6-dimethylbenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
96% inhibition at 0.1 mM
(E)-4-(2-(5,6-dimethylbenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
-
-
(E)-4-(2-(5-bromobenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
82% inhibition at 0.1 mM
(E)-4-(2-(5-bromobenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
-
-
(E)-4-(2-(5-chlorobenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
89% inhibition at 0.1 mM
(E)-4-(2-(5-chlorobenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
-
-
(E)-4-(2-(6-bromobenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
21% inhibition at 0.1 mM
(E)-4-(2-(6-bromobenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
-
-
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-2-chloro-N,N-diethylbenzenesulfonamide
12% inhibition at 0.1 mM
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-2-chloro-N,N-diethylbenzenesulfonamide
-
-
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-diethyl-2-fluorobenzenesulfonamide
18% inhibition at 0.1 mM; 28% inhibition at 0.1 mM
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-diethyl-2-fluorobenzenesulfonamide
-
-
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-diethyl-2-methylbenzenesulfonamide
30% inhibition at 0.1 mM
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-diethyl-2-methylbenzenesulfonamide
-
-
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
competitive inhibition, complete inhibition at 0.1 mM
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
-
-
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-dimethylbenzenesulfonamide
14% inhibition at 0.1 mM
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-dimethylbenzenesulfonamide
-
-
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-(4-methoxyphenyl)benzenesulfonamide
28% inhibition at 0.1 mM
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-(4-methoxyphenyl)benzenesulfonamide
-
-
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-(4-methylbenzyl)benzenesulfonamide
33% inhibition at 0.1 mM
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-(4-methylbenzyl)benzenesulfonamide
-
-
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-benzylbenzenesulfonamide
11% inhibition at 0.1 mM
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-benzylbenzenesulfonamide
-
-
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-phenylbenzenesulfonamide
25% inhibition at 0.1 mM
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N-phenylbenzenesulfonamide
-
-
(E)-N,N-diethyl-4-(2-(5-fluorobenzo[d]thiazol-2-yl)vinyl)benzenesulfonamide
84% inhibition at 0.1 mM
(E)-N,N-diethyl-4-(2-(5-fluorobenzo[d]thiazol-2-yl)vinyl)benzenesulfonamide
-
-
(E)-N,N-diethyl-4-(2-(5-methoxybenzo[d]thiazol-2-yl)vinyl)benzenesulfonamide
13% inhibition at 0.1 mM
(E)-N,N-diethyl-4-(2-(5-methoxybenzo[d]thiazol-2-yl)vinyl)benzenesulfonamide
-
-
(E)-N,N-diethyl-4-(2-(5-methylbenzo[d]thiazol-2-yl)vinyl)benzenesulfonamide
14% inhibition at 0.1 mM
(E)-N,N-diethyl-4-(2-(5-methylbenzo[d]thiazol-2-yl)vinyl)benzenesulfonamide
-
-
1-(4-(4-chlorophenyl)thiazol-2-yl)-2-(propan-2-ylidene)hydrazine
-
i.e. BF1, shows substrate selectivity for histone H3 acetylation and inhibitory activity in vitro on recombinant HATs Gcn5 and p300. Both global acetylation of histone H3 and specific acetylation at lysine 18 (H3AcK18) are lowered by BF1 treatment
1-(4-(4-chlorophenyl)thiazol-2-yl)-2-(propan-2-ylidene)hydrazine
-
i.e. BF1, shows substrate selectivity for histone H3 acetylation and inhibitory activity in vitro on recombinant HATs Gcn5 and p300. Both global acetylation of histone H3 and specific acetylation at lysine 18 (H3AcK18) are lowered by BF1 treatment
2,6-bis(3-bromo-4-hydroxybenzylidene)cyclohexanone
-
-
2,6-bis(3-bromo-4-hydroxybenzylidene)cyclohexanone
RC56, specific inhibitor, complete inhibition at 0.1 mM
2,6-bis(3-bromo-4-hydroxybenzylidene)cyclohexanone
-
RC56, cinnamoyl-III
2-(2-cyclopentylidenehydrazinyl)-4-(4-fluorophenyl)-1,3-thiazole
-
2-(2-cyclopentylidenehydrazinyl)-4-(4-fluorophenyl)-1,3-thiazole
-
-
2-butyl-6-hydroxybenzoic acid
-
2-butyl-6-hydroxybenzoic acid
-
-
2-fluoro-N'-(naphthalene-2-sulfonyl)benzohydrazide
-
CTx-0124143
2-fluoro-N'-(naphthalene-2-sulfonyl)benzohydrazide
i.e. CTX-0124143, a reversible Ac-CoA-competitive inhibitor of KAT6A
2-hydroxy-6-(11-hydroxyundecyl)benzoic acid
-
2-hydroxy-6-(11-hydroxyundecyl)benzoic acid
-
-
2-hydroxy-6-pentadecylbenzoic acid
i.e. anacardic acid, 97% inhibition at 0.05 mM
2-hydroxy-6-pentadecylbenzoic acid
-
2-[2-(4-heptylphenyl)ethyl]-6-hydroxybenzoic acid
complete inhibition at 0.05 mM
2-[2-(4-heptylphenyl)ethyl]-6-hydroxybenzoic acid
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
3-quinolinecarboxylic acid ethyl ester
-
effects in vivo, overview
3-quinolinecarboxylic acid ethyl ester
-
effects in vivo, inhibitory effect on the transcription is not fully GCN5-specific, overview
4-(4-bromophenyl)-2-[2-(propan-2-ylidene)hydrazinyl]-1,3-thiazole
-
4-(4-bromophenyl)-2-[2-(propan-2-ylidene)hydrazinyl]-1,3-thiazole
-
-
4-(4-chlorophenyl)-2-(2-cyclopentylidenehydrazinyl)-1,3-thiazole
-
CPTH2
4-(4-chlorophenyl)-2-(2-cyclopentylidenehydrazinyl)-1,3-thiazole
-
4-acetyl-2-methyl-N-(morpholin-4-yl)-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
-
4-acetyl-2-methyl-N-(morpholin-4-yl)-3,4-dihydro-2H-1,4-benzothiazine-7-sulfonamide
-
4-hydroxy-2-pentylquinoline-3-carboxylic acid
-
-
4-hydroxy-2-pentylquinoline-3-carboxylic acid
-
MC1823
4-hydroxy-2-pentylquinoline-3-carboxylic acid
-
4-hydroxy-2-pentylquinoline-3-carboxylic acid
-
-
5-chloro-2-ethylisothiazol-3(2H)-one
-
5-chloro-2-ethylisothiazol-3(2H)-one
-
-
A-485
-
A-485
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
acetylated histone H3 peptide
-
acetylated at Lys14, product inhibition of PCAF protein, noncompetitive against both substrates
-
acetylated histone H3 peptide
-
noncompetitive versus acetyl-CoA and histone H3
-
anacardic acid
-
anacardic acid
-
anarcardic acid supresses TNF-induced HAT activity
anacardic acid
-
10 microM inhibit histidine-tagged recombinant p300 with purified human HeLa core histone as substrate by about 95%
anacardic acid
-
a p300HAT inhibitor
anacardic acid
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
anacardic acid
-
reversibly and noncompetitively inhibits HAT activity with a 50% inhibitory concentration of 0.03 nM. The parasiticidal effect of anacardic acid is at least partially associated with its inhibition of PfGCN5 HAT, resulting in the disturbance of the transcription program in the parasites
bisubstrate analogue histone H3-peptide-coenzyme A
-
potent inhibitor, competitive versus acetyl-CoA, non-competitive versus histone H3-peptide
-
bisubstrate analogue histone H3-peptide-coenzyme A
-
peptide consisting of 20 and 7 amino acid residues
-
bisubstrate analogue histone H3-peptide-coenzyme A
-
-
-
Brij-58
-
-
C646
-
C646
CBP/p300-specific histone acetyltransferase inhibitor, that inhibits proliferation of hepatocellular carcinoma cell lines in a dose-dependent manner; CBP/p300-specific histone acetyltransferase inhibitor, that inhibits proliferation of hepatocellular carcinoma cell lines in a dose-dependent manner
C646
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
Ca2+
-
-
Ca2+
-
Mg2+ or Ca2+ required at low concentration of 5 mM, inhibition at 10-20 mM
CoA
-
-
CoA
-
product inhibition of PCAF protein, competitive against acetyl-CoA
CoA
-
competitive versus acetyl-CoA, Gnc5 protein
CoA
CoA binds competitively with acetyl-CoA
CPTH2
-
CPTH2
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
curcumin
Herpes simplex virus
-
curcumin affects VP16-mediated recruitment of RNA polymerase II to IE gene promoters by a mechanism independent of p300/CBP histone acetyltransferase activity
curcumin
-
increase in eNOS mRNA, caused by shear stress, is completely blocked by p300 small interfering RNA; increase in eNOS mRNA, caused by shear stress, is completely blocked by pharmacological inhibition of p300/HAT activity with curcumin
curcumin
-
25 microM inhibit histidine-tagged recombinant p300 with purified human HeLa core histone as substrate by about 75%
curcumin
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
desulfo-coenzyme A
-
dead-end inhibitor, noncompetitive versus histone H3-peptide and competitive versus actyl-CoA
desulfo-coenzyme A
-
dead-end inhibitor, competitive versus acetyl-CoA, Gcn5 protein
DNA
-
dsDNA
DNA
-
acetylation of histone H1by the enzymes PCAF and GNC5 is inhibited in vivo by complexing of H1 with DNA
DNA
-
added DNA forming complexes with the histones inhibits activity
DNA
-
in vitro, enzyme form A inhibited, enzyme form B relatively insensitive
DNA
-
enzyme form A activated by low concentrations, enzyme form B inhibited
EDTA
-
weak
EDTA
-
high concentrations
epigallocatechin-3-gallate
-
epigallocatechin-3-gallate
-
-
epigallocatechin-3-gallate
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 EGCG; EGCG; EGCG
ethyl 2-methyl-6-([5-[(prop-2-yn-1-yl)amino]pentyl]oxy)quinoline-3-carboxylate
-
-
ethyl 2-methyl-6-([5-[(prop-2-yn-1-yl)amino]pentyl]oxy)quinoline-3-carboxylate
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
ethyl 2-methylquinoline-3-carboxylate
-
effects in vivo, overview
ethyl 2-methylquinoline-3-carboxylate
-
MC1626
ethyl 2-methylquinoline-3-carboxylate
-
effects in vivo, inhibitory effect on the transcription is fully GCN5-specific, overview
Fe2+
-
-
Fe2+
-
5 mM, enzyme form B
garcinol
-
-
garcinol
-
10 microM inhibit histidine-tagged recombinant p300 with purified human HeLa core histone as substrate by about 80%
garcinol
competitive inhibitor versus both acetyl-CoA and histone, docking to the p300 HAT domain encompasses amino acid residues 1284-1673, and inhibition mechanism, overview. Also inhibits PCAF HAT activity, 90% inhibition at 0.04 mM
garcinol
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
garcinol
after induction of hind limb ischemia, blood flow recovery is impaired in both PCAF-/- mice and healthy wild type mice treated with the pharmacological PCAF inhibitor garcinol
garcinol
-
both the acetylation and induction of the inflammatory proteins in elevated glucose levels are significantly inhibited by inhibitors of histone acetyltransferase, such as garcinol and antisense against the histone acetylase, p300
garcinol
garcinaol inhibits TgGCN5b and mediates changes in the parasite transcriptome. Treatment of tachyzoites with garcinol leads to a reduction of global lysine acetylation, particularly on histone H3 and TgGCN5b itself
garcinol
isolated from Garcinia indica, inhibits GCN5-mediated lysine acetyltransferase activity and prevents the replication of the parasite. Treatment of tachyzoites with garcinol leads to a reduction of global lysine acetylation, particularly on histone H3 and TgGCN5b itself. transcriptome sequencing (RNA-seq), which reveals increasing aberrant gene expression coincident with increasing concentrations of garcinol. The majority of the genes that are most significantly affected by garcinol are also associated with TgGCN5b in a previously reported chromatin immunoprecipitation assay with microarray technology analysis. The dysregulated gene expression induced by garcinol significantly inhibits Toxoplasma tachyzoite replication, and the concentrations used exhibit no overt toxicity on human host cells. Garcinol also reduces autoacetylation of TgGCN5b, garcinol treatment results in a 65% reduction in the acetylation level of HA-tagged TgGCN5b. Garcinol-mediated changes in the parasite transcriptome, overview
H3-CoA-20
-
-
H3-CoA-20
-
IC50: 0.034-0.064 mM
histone
-
histone H1 acetylation is inhibited by all other histone fractions
histone
-
histones H2A, H2B, and H3
histone
-
inhibits spermidine acetylation, enzyme forms A and B
iodoacetamide
-
enzyme form A is more sensitive than enzyme form B
isogarcinol
-
10 microM inhibit histidine-tagged recombinant p300 with purified human HeLa core histone as substrate by about 70%
isogarcinol
competitive inhibitor versus both acetyl-CoA and histone, docking to the p300 HAT domain encompasses amino acid residues 1284-1673, and inhibition mechanism, overview. Also inhibits PCAF HAT activity to maximally 50%
isogarcinol
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
isothiazolone
-
-
isothiazolone
-
binds irreversibly to proteins via thiol interactions
K+
-
strong
K+
-
175 mM: 50% inhibition
LTK14
-
20 microM inhibit histidine-tagged recombinant p300 with purified human HeLa core histone as substrate by about 70%
LTK14
noncompetitive inhibitor versus both acetyl-CoA and histone, docking to the p300 HAT domain encompasses amino acid residues 1284-1673, and inhibition mechanism, overview
Lys-CoA
-
autoacetylation IC50: 100 nM, below
Lys-CoA
-
IC50: 310-420 nM
Lys-CoA
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
MB-3
-
-
MB-3
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 an alpha-methylene-gamma-butyrolactone, shows reversible, noncovalent mode of inhibition; an alpha-methylene-gamma-butyrolactone, shows reversible, noncovalent mode of inhibition
methyl 3-(5-chloro-1-oxido-3-oxoisothiazol-2(3H)-yl)propanoate
-
methyl 3-(5-chloro-1-oxido-3-oxoisothiazol-2(3H)-yl)propanoate
-
-
MG149
complete inhibition at 0.05 mM
Mg2+
-
-
Mg2+
-
Mg2+ or Ca2+ required at low concentration, 5 mM, inhibition at 10-20 mM
Mg2+
-
37 mM: 50% inhibition
Mn2+
-
-
N'-(3-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(pyrimidin-5-yl)benzoyl)benzenesulfonohydrazide
-
N'-(3-(pyrimidin-5-yl)benzoyl)benzenesulfonohydrazide
-
N'-(benzenesulfonyl)-4-fluoro-5-methyl[1,1'-biphenyl]-3-carbohydrazide
-
WM-8014
N'-(benzenesulfonyl)-4-fluoro-5-methyl[1,1'-biphenyl]-3-carbohydrazide
-
N-(4-[[(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)methyl](prop-2-yn-1-yl)amino]benzoyl)-L-glutamic acid
-
-
N-(4-[[(2-amino-4-oxo-3,4-dihydroquinazolin-6-yl)methyl](prop-2-yn-1-yl)amino]benzoyl)-L-glutamic acid
ZINC19217280
N-ethylmaleimide
-
enzyme form A is more sensitive than enzyme form B
N-[(4-fluorophenyl)methyl]-2-[(1R)-5-[(methylcarbamoyl)amino]-2',4'-dioxo-2,3-dihydrospiro[indene-1,5'-[1,3]oxazolidin]-3'-yl]-N-[(2S)-1,1,1-trifluoropropan-2-yl]acetamide
-
A-485
N-[(4-fluorophenyl)methyl]-2-[(1R)-5-[(methylcarbamoyl)amino]-2',4'-dioxo-2,3-dihydrospiro[indene-1,5'-[1,3]oxazolidin]-3'-yl]-N-[(2S)-1,1,1-trifluoropropan-2-yl]acetamide
-
Na+
-
strong
Na+
-
competitive against both acetyl-CoA and histones
Na+
-
160 mM: 50% inhibition
NU9056
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
NU9056
causes decreased acetylation level of histone H4 in mammalian cells
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
strongly inhibits activity of enzyme form B, formation of acyl-enzyme complex
p-chloromercuribenzoate
-
enzyme form B less sensitive than enzyme form A
Plumbagin
-
RTK1, naturally occurring hydroxynaphthoquinone, isolated from Plumbago rosea roots, inhibits histone acetylation, and induces apoptosis at higher concentrations, it inhibits p300/CBP-mediated acetylation of p53 lysine 373 non-competitively, 25 microM inhibit histidine-tagged recombinant p300 with purified human HeLa core histone as substrate by about 60% compared to control; RTK1, naturally occurring hydroxynaphthoquinone, isolated from Plumbago rosea roots, it does not inhibit PCAF acetylation of p53 lysine 320 in vivo in HEK-293 cells (pretreated with acetylation inducer doxorubicin), but 10, 25, and 50 microM inhibit FLAG-tagged recombinant PCAF in vitro (30°C) with purified human HeLa core histone as substrate
Plumbagin
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 -
Plumbagin
-
RTK1, naturally occurring hydroxynaphthoquinone, isolated from Plumbago rosea roots
protein HBZ
HTLV-1 (basic zipper factor, from a human T cell leukemia virus), interacts with HBO1 during pathogenesis and inhibits its acetylation activity to reduce p53-mediated transcription activation of p21/CDKN1A and Gadd45a, and subsequently delays G2-cell cycle arrest. BRPF2 binds to HBO1 on the hinge connecting the NTD and MYST domain, thus it is reasonable to develop BRPF2-mimic peptides or molecules for disrupting HBO1-BRPF2 interaction and subsequently prevent the binding of HBO1 to chromatin
-
protein HBZ
HTLV-1 (basic zipper factor, from a human T cell leukemia virus), interacts with HBO1 during pathogenesis and inhibits its acetylation activity to reduce p53-mediated transcription activation of p21/CDKN1A and Gadd45a, and subsequently delays G2-cell cycle arrest
-
Triton X-100
-
-
Triton X-100
-
no inhibition
Zn2+
-
-
Zn2+
-
5 mM, enzyme form B
[histone H4]-L-lysine16-CoA
bisubstrate inhibitor, i.e. Ac-SGRGKGGKGLGKGGAK(CoA)RHRK
-
[histone H4]-L-lysine16-CoA
-
-
-
additional information
-
monovalent cations cause a 50% decrease in activity at an average concentration of 51 mM, divalent cations at 15 mM
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
-
additional information
-
screening for small molecule inhibitors reducing the cell growth, overview
-
additional information
-
inhibitory potency of N-substituted isothiazolone-based compounds, in vivo cell proliferation inhibition, overview
-
additional information
-
although downregulation of UHRF1 by RNA interference enhances Tip60 expression, a significant decrease of the level of acetylated H2AK5 is observed
-
additional information
-
relative inhibition of p300, CBP, GCN5, and PCAF, overview
-
additional information
5-chloroisothiazoline inhibitors: design, synthesis and study of inhibitory potencies and inhibition of cell growth, molecular modeling, overview; N-methyl-5-chloroisothiazolone/N-methylisothiazolone in a ratio of 3:1 in Kathon TM CG, a preservative in cosmetics, that inhibits PCAF and the growth of cell lines A2780 and HEK-293
-
additional information
-
inhibitory potencies of isothiazolones and isothiazolone-1-oxides on PCAF and growth inhibition of Hep-G2 cancer cells, overview
-
additional information
-
HBO1 dissociation from origins is either triggered by proteolytic degradation of a key licensing cofactor or by post-translational event(s) induced by HU and/or actinomycin D treatment(s)
-
additional information
-
no inhibition of p300 by 5-methoxy-2-methyl-1,4-naphthoquinone (RTK2, alkyl substitution of hydroxyl group), 5-ethoxy-2-methyl-1,4-naphthoquinone (RTK3, alkyl substitution of hydroxyl group), 5-isopropoxy-2-methyl-1,4-naphthoquinone (RTK4, alkyl substitution of hydroxyl group), and 5-[2-(dimethylamino)-ethoxy]-2-methyl-1,4-naphthoquinone (RTK10, N,N-dimethylamine substitution of hydroxyl group), less than 10% inhibition with 6-methyl-5,8-dioxo-5,8-dihydronaphthalen-1-yl acetate (RTK5, acetyl substitution of hydroxyl group), 6-methyl-5,8-dioxo-5,8-dihydronaphthalen-1-yl methanesulfonate (RTK6, sulfonyl substitution of hydroxyl group), 2-methyl-5-(2-piperidin-1-ylethoxy)-1,4-naphthoquinone (RTK7, piperidine substitution of hydroxyl group), 2-methyl-5-(2-morpholin-4-ylethoxy)-1,4-naphthoquinone (RTK8, morpholine substitution of hydroxyl group), and ethyl [(6-methyl-5,8-dioxo-5,8-dihydronaphthalen-1-yl)-oxy]acetate (RTK9, ester substitution of hydroxyl group)
-
additional information
effect of garcinol and its derivative on PCAF stability, overview. Isothermal titration calorimetry studies and molecular mechanisms of p300 HAT inhibition by specific and nonspecific HAT inhibitors: garcinol, isogarcinol. Residues LTK14, S1396, Y1397, G1626, and R1627 contact the inhibitors, overview
-
additional information
-
synthesis of a novel series of thiazole-based histone acetyltransferase inhibitors active both in vitro and in vivo, overview
-
additional information
no inhibition by 14, 11c, 13, 8a, and 8b; no inhibition by 2-hydroxy-5-pentylbenzoic acid, 2-hydroxy-6-(5-hydroxypentyl)benzoic acid, and (4E)-2-(4-acetylphenyl)-4-[[5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl]methylidene]-5-methyl-2,4-dihydro-3H-pyrazol-3-one
-
additional information
no inhibition by 14, 11c, 13, 8a, and 8b; no inhibition by 2-hydroxy-5-pentylbenzoic acid, 2-hydroxy-6-(5-hydroxypentyl)benzoic acid, and (4E)-2-(4-acetylphenyl)-4-[[5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl]methylidene]-5-methyl-2,4-dihydro-3H-pyrazol-3-one
-
additional information
some (thiazol-2-yl)hydrazones act as antiprotozoal, antifungal and anti-MAO agents and as well as Gcn5 HAT inhibitors
-
additional information
-
some (thiazol-2-yl)hydrazones act as antiprotozoal, antifungal and anti-MAO agents and as well as Gcn5 HAT inhibitors
-
additional information
docking of C646 and C646-yne to a structure of p300 (PDB: 3BIY) suggests the two molecules can adopt a similar conformation in the KAT active site
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
-
additional information
-
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview. No inhibition by PU141
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additional information
-
the enzyme is not inhibited by xyloside-primed GAG chains
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additional information
high-throughput screening to discover inhibitors of histone acetyltransferase KAT6A, synthesis, and structure-activity relationship analysis, inhibition parameters and bioavailability, overview
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additional information
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design, synthesis and evaluation of a set of substrate-based peptide inhibitors containing multiple binding modalities, overview. In addition to the CoA moiety and the histone H3 peptide backbone, mono- and tri-methyl marks are incorporated at Lys4 and/or Lys9 sites in the H3 peptide substrate. The biochemical assay results show that the presence of methyl group(s) on the substrate results in more potent inhibitors of Tip60, relative to the parent H3-CoA bisubstrate inhibitor, inhibitory properties of the ligands against full-length Tip60 and the HAT domain, the K4me1 and K9me3 marks contribute to the potency augmentation by interacting with the catalytic region of the enzyme. No inhibition by Ac-ARTK(me)QTARKSTGGK(Br)APRKQL, Ac-ARTKQTARKSTGGK(Sme)APRKQL and Ac-ARTKQTARK(me)3STGGK(CoA)APRKQL
-
additional information
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PPARgamma suppresses eotaxin, an NF-kappaB target, gene expression by direct inhibition of p65-associated HAT activity, for example, by competing with p65 for limited amounts of CBP and/or by recruiting HDAC to the p65-HAT complex
-
additional information
-
both the acetylation and induction of the inflammatory proteins in elevated glucose levels are significantly inhibited by inhibitors of histone acetyltransferase, such as garcinol and antisense against the histone acetylase, p300
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additional information
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screening for small molecule inhibitors reducing the cell growth, overview
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additional information
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protein factors such as E1A and Nap1 can modulate p300/CBP HAT activity
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additional information
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synthesis of a novel series of thiazole-based histone acetyltransferase inhibitors active both in vitro and in vivo, overview
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additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
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additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
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additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
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additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
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additional information
analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview; analysis of KATi, bisubstrate analogues, natural compounds and synthetic derivatives, mechanism of action, structure-activity relationships, and pharmacokinetic/pharmacodynamic properties, overview
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additional information
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effects of three monofluorinated phenylalanine analogs p-fluorophenylalanine, m-fluorophenylalanine, and o-fluorophenylalanine on the stability and enzymatic activity of tGCN5, overview
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0.0023
(2E,6E)-2,6-bis[(3,5-dibromo-4-hydroxyphenyl)methylidene]cyclohexan-1-one
Homo sapiens
at pH 8.0 and 30°C
0.0389
(2E,6E)-2,6-bis[(3-fluoro-4-hydroxyphenyl)methylidene]cyclohexan-1-one
Homo sapiens
at pH 8.0 and 30°C
0.0268
(2E,6E)-2,6-bis[(4-hydroxy-3-methylphenyl)methylidene]cyclohexan-1-one
Homo sapiens
at pH 8.0 and 30°C
0.035
(3Z,5Z)-3,5-bis[(3-bromo-4-hydroxyphenyl)methylidene]thian-4-one
Homo sapiens
at pH 8.0 and 30°C
0.00047
(4-(4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)phenyl)phosphonic acid
Homo sapiens
at pH 8.0 and 25°C
0.32
(4E)-2-(4-acetylphenyl)-4-[[5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl]methylidene]-5-methyl-2,4-dihydro-3H-pyrazol-3-one
Homo sapiens
pH and temperature not specified in the publication
0.0077
(E)-4-(2-(5,6-dimethylbenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.03
(E)-4-(2-(5-bromobenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.03
(E)-4-(2-(5-chlorobenzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.006
(E)-4-(2-(benzo[d]thiazol-2-yl)vinyl)-N,N-diethylbenzenesulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.04
(E)-N,N-diethyl-4-(2-(5-fluorobenzo[d]thiazol-2-yl)vinyl)benzenesulfonamide
Homo sapiens
at pH 7.5 and 25°C
0.005
1,7-bis(3-bromo-4-hydroxyphenyl)-1,6-heptadiene-3,5-dione
Homo sapiens
-
-
0.0071
2'-chloro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00062
2'-fluoro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0082
2'-methoxy-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00023
2,3-difluoro-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00018
2,4-difluoro-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0309 - 0.033
2,6-bis(3-bromo-4-hydroxybenzylidene)cyclohexanone
0.0455
2,6-bis(3-chloro-4-hydroxybenzylidene)cyclohexan-1-one
Homo sapiens
at pH 8.0 and 30°C
0.0081
2,6-bis(4-hydroxy-3-iodobenzylidene)cyclohexan-1-one
Homo sapiens
at pH 8.0 and 30°C
0.00018
2,6-difluoro-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00731
2-(3,5-difluoro-4-hydroxyphenyl)-4-((5-(4,5-dimethyl-2-(trifluoromethyl)phenyl)furan-2-yl)methylene)-5-methyl-2,4-dihydro-3H-pyrazol-3-one
Homo sapiens
at pH 8.0 and 25°C
0.0048
2-(3,5-difluoro-4-hydroxyphenyl)-4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-5-methyl-2,4-dihydro-3H-pyrazol-3-one
Homo sapiens
at pH 8.0 and 25°C
0.01
2-(3,5-difluoro-4-hydroxyphenyl)-5-methyl-4-((5-(2-(trifluoromethoxy)phenyl)furan-2-yl)methylene)-2,4-dihydro-3H-pyrazol-3-one
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 25°C
0.00373 - 0.00605
2-(3,5-difluoro-4-hydroxyphenyl)-5-methyl-4-((5-(3-oxo-2,3-dihydro-1H-inden-4-yl)furan-2-yl)methylene)-2,4-dihydro-3H-pyrazol-3-one
0.0024
2-(3-fluoro-5-(2-((2-fluorophenyl)sulfonyl)hydrazinecarbonyl)-phenyl)pyridine 1-Oxide
Homo sapiens
pH and temperature not specified in the publication
0.00503
2-(3-methoxyphenyl)isothiazolo[5,4-b]pyridin-3(2H)-one
Homo sapiens
-
substrate histone H3 peptide, pH 7.5, 30°C
0.00067
2-(4-(2H-tetrazol-5-yl)phenyl)-4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-5-methyl-2,4-dihydro-3H-pyrazol-3-one
Homo sapiens
at pH 8.0 and 25°C
0.0255 - 0.13
2-(4-(trifluoromethyl)benzyl)isothiazolo[5,4-b]pyridin-3(2H)-one
0.00072 - 0.00164
2-(4-fluorophenyl)isothiazolo[5,4-b]pyridin-3(2H)-one
0.00463
2-(4-methylphenyl)isothiazolo[5,4-b]pyridin-3(2H)-one
Homo sapiens
-
substrate histone H3 peptide, pH 7.5, 30°C
0.125
2-chloro-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
Mus musculus
IC50 above 0.125 mM, in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.0073
2-cyano-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00053
2-fluoro-3-hydroxy-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00039
2-fluoro-3-methyl-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00012
2-fluoro-4-methyl-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00023
2-fluoro-5-hydroxy-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000073
2-fluoro-5-methoxy-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000096
2-fluoro-5-methyl-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00011
2-fluoro-6-methoxy-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000062
2-fluoro-N'-(2-fluoro-5-methyl-3-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000044
2-fluoro-N'-(2-fluoro-5-methyl-3-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00169
2-fluoro-N'-(2-phenylisonicotinoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000018
2-fluoro-N'-(3-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000029
2-fluoro-N'-(3-(4-fluoro-1H-pyrazol-1-yl)-5-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00034
2-fluoro-N'-(3-(4-fluoro-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0003
2-fluoro-N'-(3-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00002
2-fluoro-N'-(3-(furan-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000006
2-fluoro-N'-(3-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000025
2-fluoro-N'-(3-(thiophen-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000014
2-fluoro-N'-(3-(thiophen-3-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00027
2-fluoro-N'-(3-fluoro-5-(1H-pyrazol-1-yl)benzoyl)-3-methoxybenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00035
2-fluoro-N'-(3-fluoro-5-(1H-pyrazol-1-yl)benzoyl)-4-methoxybenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000026
2-fluoro-N'-(3-fluoro-5-(1H-pyrazol-1-yl)benzoyl)-5-hydroxybenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0001
2-fluoro-N'-(3-fluoro-5-(1H-pyrazol-1-yl)benzoyl)-5-methoxybenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000009
2-fluoro-N'-(3-fluoro-5-(2H-1,2,3-triazol-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000023
2-fluoro-N'-(3-fluoro-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000032
2-fluoro-N'-(3-fluoro-5-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000031
2-fluoro-N'-(3-fluoro-5-(5-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00027
2-fluoro-N'-(3-fluoro-5-(pyridin-2-yl)benzoyl)-3-hydroxybenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0000063
2-fluoro-N'-(3-fluoro-5-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00006
2-fluoro-N'-(3-iodobenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000017 - 0.08
2-fluoro-N'-(3-isobutoxybenzoyl)benzenesulfonohydrazide
0.059
2-fluoro-N'-(3-isopropoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00097
2-fluoro-N'-(3-isopropylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000013
2-fluoro-N'-(3-methoxy-5-(1H-pyrazol-1-yl)benzoyl)-benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000203
2-fluoro-N'-(3-methoxy-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000024
2-fluoro-N'-(3-methoxy-5-(pyrimidin-2-yl)benzoyl)-benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000027
2-fluoro-N'-(3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000018
2-fluoro-N'-(3-methyl-5-(2H-1,2,3-triazol-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000007
2-fluoro-N'-(3-methyl-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000014
2-fluoro-N'-(3-methyl-5-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000013
2-fluoro-N'-(3-methyl-5-(5-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00038
2-fluoro-N'-(3-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.094
2-fluoro-N'-(3-propoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000094
2-fluoro-N'-(3-propylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00235
2-fluoro-N'-(5-phenylnicotinoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0029
2-fluoro-N'-(6-phenylpicolinoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.001
2-fluoro-N'-(naphthalene-2-sulfonyl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0018
2-fluoro-N'-(phenylsulfonyl)benzohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0041 - 0.0057
2-fluoro-N'-[(3-fluorophenyl)sulfonyl]benzohydrazide
0.0044
2-fluoro-N'-[[3-(trifluoromethyl)phenyl]sulfonyl]benzohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.049
2-hydroxy-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.01
2-tert-butyl-5-(dodecylthio)isothiazol-3(2H)-one-1-oxide
Homo sapiens
-
above
0.01
2-tert-butyl-5-chloroisothiazol-3(2H)-one 1-oxide
Homo sapiens
-
above
0.015
2-[2-(4-heptylphenyl)ethyl]-6-hydroxybenzoic acid
Homo sapiens
at pH 7.5 and 25°C
0.00079
3'-chloro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0034
3'-cyano-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.011
3'-fluoro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.009
3'-methoxy-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.012
3-(2-(2-fluorobenzoyl)hydrazinylsulfono)benzamide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00049
3-amino-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0036
3-bromo-N'-(3-ethoxybenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0017
3-chloro-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00052
3-chloro-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.014
3-cyano-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000023
3-fluoro-N'-(2-fluorobenzene-1-sulfonyl)-5-(1H-pyrazol-1-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0000094
3-fluoro-N'-(2-fluorobenzene-1-sulfonyl)-5-(furan-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000014
3-fluoro-N'-(2-fluorobenzene-1-sulfonyl)-5-(pyrimidin-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0013
3-fluoro-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0014
3-methyl-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.004
4'-chloro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.041
4'-cyano-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0095
4'-fluoro-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0258
4'-methoxy-N'-(phenylsulfonyl)biphenyl-3-carbohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0024
4,5-dichloro-2-ethylisothiazol-3(2H)-one
Homo sapiens
-
-
0.01
4,5-dichloro-2-ethylisothiazol-3(2H)-one-1-oxide
Homo sapiens
-
above
0.00406
4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-5-methyl-2-(4-(methylsulfonyl)phenyl)-2,4-dihydro-3H-pyrazol-3-one
Homo sapiens
at pH 8.0 and 25°C
0.00016
4-(3-cyclopropyl-4-((5-(4,5-dimethyl-2-(trifluoromethyl)phenyl)thiophen- 2-yl)methylene)-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.0002
4-(3-cyclopropyl-4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.00056
4-(3-methyl-4-((5-(2-nitrophenyl)furan-2-yl)methylene)-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.00113
4-(3-methyl-5-oxo-4-((5-(2-(trifluoromethoxy)phenyl)furan-2-yl)methylene)-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.00058
4-(3-methyl-5-oxo-4-((5-(3-oxo-2,3-dihydro-1H-inden-4-yl)furan-2-yl)methylene)-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.00086
4-(4-((2-(4,5-dimethyl-2-nitrophenyl)thiazol-5-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.00117
4-(4-((5-(2-(difluoromethyl)phenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.01
4-(4-((5-(2-(dimethylphosphoryl)phenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 25°C
0.00029
4-(4-((5-(4,5-dimethyl-2-(trifluoromethyl)phenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.00195
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)-1H-pyrrol-2-yl)methylene)-3-methyl-5-oxo-4, 5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.01
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-2,5-dioxoimidazolidin-1-yl)benzoic acid
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 25°C
0.00019
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-3-ethyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.00023
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 37°C
0.00153
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzonitrile
Homo sapiens
at pH 8.0 and 25°C
0.00023
4-(4-((5-(4,5-dimethyl-2-nitrophenyl)thiophen-2-yl)methylene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.00207
4-(4-(1-(5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)ethylidene)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.00961
4-(4-(2-((4,5-dimethyl-2-nitrophenyl)amino)-2-oxoethyl)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.01
4-(4-(3-((4,5-dimethyl-2-nitrophenyl)amino)-3-oxopropyl)-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl)benzoic acid
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 25°C
0.01
4-(5-((5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl)methylene)-2,4- dioxothiazolidin-3-yl)benzoic acid
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 25°C
0.01
4-(5-(4,5-dimethyl-2-nitrobenzoyl)-1H-indazol-1-yl)benzoic acid
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 25°C
0.01
4-(5-(4,5-dimethyl-2-nitrobenzoyl)-1H-indol-1-yl)benzoic acid
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 25°C
0.01
4-(5-(4,5-dimethyl-2-nitrobenzyl)-1H-indazol-1-yl)benzoic acid
Homo sapiens
IC50 above 0.01 mM, at pH 8.0 and 25°C
0.00713
4-([(2E)-2-cyano-3-[5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl]prop-2-enoyl]amino)benzoic acid
Homo sapiens
at pH 8.0 and 25°C
0.0097
4-amino-1-naphthol
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.0125
4-amino-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
Mus musculus
IC50 above 0.0125 mM, in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.125
4-butoxy-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
Mus musculus
IC50 above 0.125 mM, in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.06
4-chloro-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
Mus musculus
in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.0125
4-cyano-N'-(2-fluorobenzoyl)benzenesulfonohydrazide
Mus musculus
IC50 above 0.0125 mM, in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.03
4-hydroxy-N'-(naphthalen-2-ylsulfonyl)benzohydrazide
Mus musculus
in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.0141
4-[(4Z)-4-[[5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]-N-(prop-2-yn-1-yl)benzamide
Homo sapiens
pH and temperature not specified in the publication
0.0068
4-[(4Z)-4-[[5-(4,5-dimethyl-2-nitrophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzoic acid
Homo sapiens
pH and temperature not specified in the publication
0.00053
5-bromo-N'-(3-ethoxybenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.01
5-chloro-2-ethyl-4-methylisothiazol-3(2H)-one
Homo sapiens
-
above
0.01
5-chloro-2-ethyl-4-methylisothiazol-3(2H)-one-1-oxide
Homo sapiens
-
above
0.003
5-chloro-2-ethylisothiazol-3(2H)-one
Homo sapiens
-
-
0.01
5-chloro-2-ethylisothiazol-3(2H)-one-1-oxide
Homo sapiens
-
above
0.0000026 - 0.0000098
A-485
0.00033 - 0.0038
Ac-ARTK(me)QTARK(me)3STGGK(CoA)APRKQL
0.0011 - 0.0345
Ac-ARTK(me)QTARKSTGGK(CoA)APRKQL
0.00028 - 0.0012
Ac-ARTKQTARK(me)3STGGK(Sme)APRKQL
0.00035 - 0.009
Ac-ARTKQTARKSTGGK(Br)APRKQL
0.0084 - 0.0091
Ac-ARTKQTARKSTGGK(CoA)APRKQL
0.0749
Ac-L-Lys(CoA)-NH2
Homo sapiens
at pH 8.0 and 30°C
0.026 - 0.348
anacardic acid
0.0016
C646
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.0022 - 0.0073
CCT077791
Homo sapiens
-
IC50: 0.0022-0.0073 mM, in vivo cell proliferation inhibition, reduces acetylation of histones H3 and H4 and alpha-tubulin in cancer cell lines
0.0027 - 0.015
CCT077792
Homo sapiens
-
IC50: 0.0027-0.015 mM, in vivo cell proliferation inhibition
0.0187 - 0.0202
CCT077796
Homo sapiens
-
IC50: 0.0187-0.0202 mM, in vivo cell proliferation inhibition
0.0547
CCT079769
Homo sapiens
-
IC50: 0.0547 mM, in vivo cell proliferation inhibition
0.0415
CoA
Homo sapiens
at pH 8.0 and 30°C
0.001 - 0.012
CTX-0124143
0.0072
embelin
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.03 - 0.07
epigallocatechin-3-gallate
0.0575
ethyl 2-methyl-6-([5-[(prop-2-yn-1-yl)amino]pentyl]oxy)quinoline-3-carboxylate
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.034 - 0.064
H3-CoA-20
Homo sapiens
-
IC50: 0.034-0.064 mM
0.012
H3-CoA-20-Tat
Homo sapiens
-
IC50: 0.012 mM, recombinant enzyme
-
0.00025
Lys-CoA-Tat
Homo sapiens
-
IC50: 250 nM, recombinant enzyme, complete inhibition of acetylation of the promyelotic leukemia zinc finger gene
0.1
MB-3
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.01
methyl 3-(4,5-dichloro-1-oxido-3-oxoisothiazol-2(3H)-yl)propanoate
Homo sapiens
-
above
0.0026
methyl 3-(4,5-dichloro-3-oxoisothiazol-2(3H)-yl)propanoate
Homo sapiens
-
-
0.0056
methyl 3-(5-chloro-1-oxido-3-oxoisothiazol-2(3H)-yl)propanoate
Homo sapiens
-
-
0.0018
methyl 3-(5-chloro-3-oxoisothiazol-2(3H)-yl)propanoate
Homo sapiens
-
-
0.01
methyl 3-(5-chloro-4-methyl-1-oxido-3-oxoisothiazol-2(3H)-yl)propanoate
Homo sapiens
-
above
0.01
methyl 3-(5-chloro-4-methyl-3-oxoisothiazol-2(3H)-yl)propanoate
Homo sapiens
-
above
0.01
methyl 3-[4-chloro-5-(dodecylthio)-1-oxido-3-oxoisothiazol-2(3H)-yl]propanoate
Homo sapiens
-
above
0.01
methyl 3-[5-(dodecylthio)-1-oxido-3-oxoisothiazol-2(3H)-yl] propanoate
Homo sapiens
-
above
0.00027
N'-( 2-fluoro-[1,1'- biphenyl]-3-carbonyl)-benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00074
N'-(2,3-difluorobenzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00013
N'-(2,3-difluorobenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000072
N'-(2,6-difluorobenzene-1-sulfonyl)-3-fluoro-5-propoxybenzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000061
N'-(2,6-difluorobenzene-1-sulfonyl)-3-fluoro-5-[(propan-2-yl)oxy]benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00011
N'-(2,6-difluorobenzene-1-sulfonyl)-3-methoxy-5-[(propan-2-yl)oxy]benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000015
N'-(2,6-difluorobenzene-1-sulfonyl)-3-methyl-5-[(propan-2-yl)oxy]benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0125
N'-(2-dluorobenzoyl)-4-methylbenzenesulfonohydrazide
Mus musculus
IC50 above 0.0125 mM, in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00039
N'-(2-fluoro-3-(trifluoromethyl)benzoyl)-benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000077
N'-(2-fluoro-3-(trifluoromethyl)benzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00049
N'-(2-fluoro-3-methoxybenzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000017
N'-(2-fluoro-3-methyl-5-((2-methylallyl)oxy)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000078
N'-(2-fluoro-3-methyl-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000096
N'-(2-fluoro-3-methyl-5-(2H-1,2,3-triazol-2-yl)benzoyl)-naphthalene-2-sulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000065
N'-(2-fluoro-3-methyl-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000084
N'-(2-fluoro-3-methyl-5-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000087
N'-(2-fluoro-3-methyl-5-(5-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00023
N'-(2-fluoro-3-methylbenzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00012
N'-(2-fluoro-3-methylbenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00014
N'-(2-fluoro-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00034
N'-(2-fluoro-5-(2H-1,2,3-triazol-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00016
N'-(2-fluoro-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000052
N'-(2-fluoro-5-(4-fluoro-1H-pyrazol-1-yl)-3-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00022
N'-(2-fluoro-5-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00008
N'-(2-fluoro-5-(furan-2-yl)-3-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00012
N'-(2-fluoro-5-(furan-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00009
N'-(2-fluoro-5-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000063
N'-(2-fluoro-5-isopropoxy-3-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000062
N'-(2-fluoro-5-isopropoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00091
N'-(2-fluoro-5-methylbenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000081
N'-(2-fluoro-5-propoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00011
N'-(2-fluorobenzene-1-sulfonyl)-3-(furan-2-yl)-5-methoxybenzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000011
N'-(2-fluorobenzene-1-sulfonyl)-3-(furan-2-yl)-5-methylbenzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00023
N'-(2-fluorobenzene-1-sulfonyl)-3-(naphthalen-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000054
N'-(2-fluorobenzene-1-sulfonyl)-3-(pyrimidin-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0019
N'-(2-fluorobenzene-1-sulfonyl)-3-(pyrimidin-4-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.56
N'-(2-fluorobenzene-1-sulfonyl)-3-(trifluoromethoxy)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000005
N'-(2-fluorobenzene-1-sulfonyl)-3-methoxy-5-(pyridin-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000008
N'-(2-fluorobenzene-1-sulfonyl)-3-methyl-5-(pyridin-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000009
N'-(2-fluorobenzene-1-sulfonyl)-3-methyl-5-(pyrimidin-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.8
N'-(2-fluorobenzene-1-sulfonyl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.017
N'-(2-fluorobenzoyl)-2-methoxybenzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0062
N'-(2-fluorobenzoyl)-2-methylbenzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0011
N'-(2-fluorobenzoyl)-3-methoxybenzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0035
N'-(2-fluorobenzoyl)-3-methylbenzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0125
N'-(2-fluorobenzoyl)-4-methoxybenzenesulfonohydrazide
Mus musculus
IC50 above 0.0125 mM, in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.042
N'-(2-methoxybenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.019
N'-(2-methylbenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.019
N'-(2-phenylisonicotinoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00049
N'-(3-(1,2,4-oxadiazol-3-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00463
N'-(3-(1,3,4-oxadiazol-2-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000043
N'-(3-(1H-pyrazol-1-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00061 - 0.125
N'-(3-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
0.00018
N'-(3-(3,5-dimethyl-1H-pyrazol-1-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0006
N'-(3-(4-fluoro-1H-pyrazol-1-yl)-5-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00002
N'-(3-(allyloxy)-5-fluorobenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000016
N'-(3-(allyloxy)-5-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.03
N'-(3-(allyloxy)benzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.23
N'-(3-(cyclopentyloxy)benzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00044
N'-(3-(cyclopentyloxy)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000091 - 0.00011
N'-(3-(cyclopropylmethoxy)-5-fluorobenzoyl)-2-fluorobenzenesulfonohydrazide
0.00009
N'-(3-(cyclopropylmethoxy)-5-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.12
N'-(3-(cyclopropylmethoxy)benzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000024
N'-(3-(ethoxymethyl)-5-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00048
N'-(3-(furan-2-yl)-5-methoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00013
N'-(3-(furan-2-yl)-5-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0074
N'-(3-(piperazin-1-yl)benzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00014
N'-(3-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.125
N'-(3-(pyridin-3-yl)benzoyl)benzenesulfonohydrazide
Mus musculus
IC50 above 0.125 mM, in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00063
N'-(3-(pyrimidin-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.029 - 0.125
N'-(3-(pyrimidin-5-yl)benzoyl)benzenesulfonohydrazide
0.00016
N'-(3-(thiazol-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00027
N'-(3-(thiazol-4-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00016
N'-(3-(thiophen-2-yl)benzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.013
N'-(3-(thiophen-3-yl)benzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.01
N'-(3-(trifluoromethoxy)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0028
N'-(3-(trifluoromethoxy)benzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.011
N'-(3-(trifluoromethyl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.011
N'-(3-(trifluoromethyl)benzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.125
N'-(3-acetylbenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
IC50 above 0.125 mM, in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.019
N'-(3-aminobenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.00018
N'-(3-bromobenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.23
N'-(3-butoxybenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.003
N'-(3-butoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00013
N'-(3-chloro-2-fluorobenzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000043
N'-(3-chloro-2-fluorobenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0000055
N'-(3-chloro-5-(furan-2-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00011
N'-(3-chloro-5-(furan-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000024
N'-(3-chloro-5-(thiophen-2-yl)benzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.024
N'-(3-cyanobenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000027
N'-(3-cyclopropoxy-5-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00011
N'-(3-ethoxy-5-fluorobenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00016
N'-(3-ethoxy-5-methoxybenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00017
N'-(3-ethoxy-5-methylbenzoyl)-2,3-difluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00013
N'-(3-ethoxy-5-methylbenzoyl)-2,4-difluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00017
N'-(3-ethoxy-5-methylbenzoyl)-2,5-difluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00013
N'-(3-ethoxy-5-methylbenzoyl)-2,6-difluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00016
N'-(3-ethoxy-5-methylbenzoyl)-2-fluoro-3-methylbenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00018
N'-(3-ethoxy-5-methylbenzoyl)-2-fluoro-4-methylbenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00012
N'-(3-ethoxy-5-methylbenzoyl)-2-fluoro-5-methylbenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000016
N'-(3-ethoxy-5-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00027
N'-(3-ethoxybenzoyl)-2-fluoro-5-methoxybenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.005
N'-(3-ethoxybenzoyl)-2-fluoro-6-methoxybenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.069
N'-(3-ethoxybenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00037
N'-(3-ethoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00057
N'-(3-ethoxybenzoyl)naphthalene-2-sulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00058
N'-(3-ethyl-2-fluorobenzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000062
N'-(3-ethyl-2-fluorobenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00022
N'-(3-ethylbenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0036
N'-(3-ethylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00044
N'-(3-fluoro-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00043
N'-(3-fluoro-5-(3-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0008
N'-(3-fluoro-5-(4-methyl-1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00014
N'-(3-fluoro-5-(furan-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0001
N'-(3-fluoro-5-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0004
N'-(3-fluoro-5-propoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0021
N'-(3-fluorobenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00024
N'-(3-isobutoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00033
N'-(3-isopropoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0062
N'-(3-isopropylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0078
N'-(3-isopropylbenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0012
N'-(3-methoxy-5-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00039
N'-(3-methoxy-5-(pyridin-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00069
N'-(3-methoxybenzoyl)naphthalene-2-sulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.018
N'-(3-methoxylbenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.0023
N'-(3-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0047
N'-(3-phenoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00038
N'-(3-propoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00012
N'-(3-propoxybenzoyl)naphthalene-2-sulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0033
N'-(3-propylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.125
N'-(4-(trifluoromethoxy)benzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
IC50 above 0.125 mM, in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.125
N'-(4-cyanobenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
IC50 above 0.125 mM, in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.000008
N'-(4-fluoro-5-methyl-[1,1'-biphenyl]-3-carbonyl)-benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000017
N'-(4-fluoro-[1,1'-biphenyl]-3-carbonyl)-benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.12
N'-(4-fluorobenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.12
N'-(4-methoxybenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.03
N'-(4-methylbenzoyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.000061
N'-(5-(allyloxy)-2-fluoro-3-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00007
N'-(5-(allyloxy)-2-fluorobenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000054
N'-(5-(cyclopropylmethoxy)-2-fluoro-3-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000029
N'-(5-(ethoxymethyl)-2-fluoro-3-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00001
N'-(5-chloro-4-fluoro-[1,1'-biphenyl]-3-carbonyl)-benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000074
N'-(5-ethoxy-2-fluoro-3-methylbenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000082
N'-(5-ethoxy-2-fluoro-3-methylbenzoyl)naphthalene-2-sulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00019
N'-(5-ethoxy-2-fluorobenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.022
N'-(5-phenylnicotinoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.018
N'-(6-phenylpicolinoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000073
N'-(benzenesulfonyl)-2-fluoro-3-methyl-5-(pyridin-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000067
N'-(benzenesulfonyl)-2-fluoro-3-methyl-5-(pyrimidin-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00014
N'-(benzenesulfonyl)-2-fluoro-5-(pyrimidin-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.125
N'-(benzenesulfonyl)-2-fluoro-5-(pyrimidin-4-yl)benzohydrazide
Homo sapiens
above, pH and temperature not specified in the publication
0.00012
N'-(benzenesulfonyl)-2-fluoro-5-[(prop-2-yn-1-yl)oxy]benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00045
N'-(benzenesulfonyl)-3-fluoro-5-(pyrimidin-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0072
N'-(benzenesulfonyl)-3-fluorobenzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00067
N'-(benzenesulfonyl)-3-methoxy-5-(pyrimidin-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0023
N'-(benzenesulfonyl)-3-methoxybenzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00023
N'-(benzenesulfonyl)-3-methyl-5-(pyrimidin-2-yl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000062
N'-(ethoxy-2-fluoro-3-methylbenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0042
N'-(naphthalen-2-ylsulfonyl)benzohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0042
N'-(naphthalene-2-sulfonyl)benzohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00014
N'-([1,1'-biphenyl]-3-carbonyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00029
N'-([1,1'-biphenyl]-3-carbonyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00088
N'-([1,1'-biphenyl]-3-carbonyl)naphthalene-2-sulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0067
N'-benzoylbenzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.001
N'-[(3-bromophenyl)sulfonyl]-2-fluorobenzohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.019
N'-[(3-ethylphenyl)sulfonyl]-2-fluorobenzohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.00046
N'-[(4-bromophenyl)sulfonyl]-2-fluorobenzohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000038
N-(2-fluoro-3-methyl-5-(2H-1,2,3-triazol-2-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.000052
N-(2-fluoro-3-methyl-5-propoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0041
N-[5-[(5-[[5-([4-[(5-[[5-([5-[(5-[[3-(dimethylamino)propyl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)amino]-4-oxobutyl]carbamoyl)-1-methyl-1H-pyrrol-3-yl]carbamoyl]-1-methyl-1H-pyrrol-3-yl)carbamoyl]-1-methyl-1H-pyrrol-3-yl]-4-[(N-[[2-(2-[4-[(4Z)-4-[[5-(2,3-dimethyl-6-nitrophenyl)furan-2-yl]methylidene]-3-methyl-5-oxo-4,5-dihydro-1H-pyrazol-1-yl]benzamido]ethoxy)ethoxy]acetyl]-beta-alanyl)amino]-1-methyl-1H-pyrrole-2-carboxamide
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.000011
NK13650A
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.000022
NK13650B
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.002
NU9056
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.00007
peptide conjugate Boc-C5-CoA
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
-
0.0003
peptide conjugate H3-CoA-20
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
-
0.00662 - 0.01759
peptide conjugate H4-K16-CoA
-
0.071
tert-butyl-(3-(2-(naphthalen-2-ylsulfono)hydrazinecarbonyl)-phenyl)carbamate
Mus musculus
in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.000002
WM-1119
Mus musculus
pH and temperature not specified in the publication
0.000008
WM-8014
Mus musculus
pH and temperature not specified in the publication
0.000023
[histone H4]-L-lysine12-CoA
Homo sapiens
at pH 8.0 and 30°C
-
0.0072
[histone H4]-L-lysine16-CoA
Homo sapiens
at pH 8.0 and 30°C
-
0.000083
[histone H4]-L-lysine5-CoA
Homo sapiens
at pH 8.0 and 30°C
-
0.0026
[histone H4]-L-lysine8-CoA
Homo sapiens
at pH 8.0 and 30°C
-
additional information
additional information
-
0.0309
2,6-bis(3-bromo-4-hydroxybenzylidene)cyclohexanone
Homo sapiens
at pH 8.0 and 30°C
0.033
2,6-bis(3-bromo-4-hydroxybenzylidene)cyclohexanone
Homo sapiens
-
-
0.00373
2-(3,5-difluoro-4-hydroxyphenyl)-5-methyl-4-((5-(3-oxo-2,3-dihydro-1H-inden-4-yl)furan-2-yl)methylene)-2,4-dihydro-3H-pyrazol-3-one
Homo sapiens
at pH 8.0 and 25°C
0.00605
2-(3,5-difluoro-4-hydroxyphenyl)-5-methyl-4-((5-(3-oxo-2,3-dihydro-1H-inden-4-yl)furan-2-yl)methylene)-2,4-dihydro-3H-pyrazol-3-one
Homo sapiens
at pH 8.0 and 25°C
0.0255
2-(4-(trifluoromethyl)benzyl)isothiazolo[5,4-b]pyridin-3(2H)-one
Homo sapiens
-
substrate histone H3 peptide, pH 7.5, 30°C
0.13
2-(4-(trifluoromethyl)benzyl)isothiazolo[5,4-b]pyridin-3(2H)-one
Homo sapiens
-
substrate histone H3 peptide, pH 7.5, 30°C
0.00072
2-(4-fluorophenyl)isothiazolo[5,4-b]pyridin-3(2H)-one
Homo sapiens
-
substrate histone H4 peptide, pH 7.5, 30°C
0.00164
2-(4-fluorophenyl)isothiazolo[5,4-b]pyridin-3(2H)-one
Homo sapiens
-
substrate histone H3 peptide, pH 7.5, 30°C
0.000017
2-fluoro-N'-(3-isobutoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.08
2-fluoro-N'-(3-isobutoxybenzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.0041
2-fluoro-N'-[(3-fluorophenyl)sulfonyl]benzohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0057
2-fluoro-N'-[(3-fluorophenyl)sulfonyl]benzohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.0000026
A-485
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.0000098
A-485
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.00033
Ac-ARTK(me)QTARK(me)3STGGK(CoA)APRKQL
Human immunodeficiency virus 1
-
pH 8.0, 30°C, catalytic subunit
0.0038
Ac-ARTK(me)QTARK(me)3STGGK(CoA)APRKQL
Human immunodeficiency virus 1
-
pH 8.0, 30°C, full-length enzyme
0.0011
Ac-ARTK(me)QTARKSTGGK(CoA)APRKQL
Human immunodeficiency virus 1
-
pH 8.0, 30°C, catalytic subunit
0.0345
Ac-ARTK(me)QTARKSTGGK(CoA)APRKQL
Human immunodeficiency virus 1
-
pH 8.0, 30°C, full-length enzyme
0.00028
Ac-ARTKQTARK(me)3STGGK(Sme)APRKQL
Human immunodeficiency virus 1
-
pH 8.0, 30°C, catalytic subunit
0.0012
Ac-ARTKQTARK(me)3STGGK(Sme)APRKQL
Human immunodeficiency virus 1
-
pH 8.0, 30°C, full-length enzyme
0.00035
Ac-ARTKQTARKSTGGK(Br)APRKQL
Human immunodeficiency virus 1
-
pH 8.0, 30°C, catalytic subunit
0.009
Ac-ARTKQTARKSTGGK(Br)APRKQL
Human immunodeficiency virus 1
-
pH 8.0, 30°C, full-length enzyme
0.0084
Ac-ARTKQTARKSTGGK(CoA)APRKQL
Human immunodeficiency virus 1
-
pH 8.0, 30°C, catalytic subunit
0.0091
Ac-ARTKQTARKSTGGK(CoA)APRKQL
Human immunodeficiency virus 1
-
pH 8.0, 30°C, full-length enzyme
0.026
anacardic acid
Plasmodium falciparum
-
inhibition of recombinant PfGCN5
0.043 - 0.348
anacardic acid
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.043 - 0.064
anacardic acid
Drosophila melanogaster
pH and temperature not specified in the publication
0.001
CTX-0124143
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.012
CTX-0124143
Mus musculus
in the presence of 0.015 mM acetyl-CoA, pH and temperature not specified in the publication
0.025
curcumin
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.4
curcumin
Homo sapiens
-
value above 0.4
0.0011
EML425
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.0029
EML425
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.03
epigallocatechin-3-gallate
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.05
epigallocatechin-3-gallate
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.06
epigallocatechin-3-gallate
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.07
epigallocatechin-3-gallate
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.005
garcinol
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.007
garcinol
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.002 - 0.128
L002
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.0339
L002
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.0347
L002
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.0001
Lys-CoA
Homo sapiens
-
autoacetylation IC50: 100 nM, below
0.00031 - 0.00042
Lys-CoA
Homo sapiens
-
IC50: 310-420 nM
0.0005
Lys-CoA
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.03
Lys-CoA
Homo sapiens
-
-
0.2
Lys-CoA
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.00061
N'-(3-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.125
N'-(3-(1H-pyrazol-1-yl)benzoyl)benzenesulfonohydrazide
Mus musculus
IC50 above 0.125 mM, in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.000091
N'-(3-(cyclopropylmethoxy)-5-fluorobenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.00011
N'-(3-(cyclopropylmethoxy)-5-fluorobenzoyl)-2-fluorobenzenesulfonohydrazide
Homo sapiens
pH and temperature not specified in the publication
0.029
N'-(3-(pyrimidin-5-yl)benzoyl)benzenesulfonohydrazide
Mus musculus
in the presence of 0.0004 mM acetyl-CoA, pH and temperature not specified in the publication
0.125
N'-(3-(pyrimidin-5-yl)benzoyl)benzenesulfonohydrazide
Homo sapiens
above, pH and temperature not specified in the publication
0.00662
peptide conjugate H4-K16-CoA
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
-
0.01759
peptide conjugate H4-K16-CoA
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
-
0.002
Plumbagin
Homo sapiens
-
recombinant minimal HAT domain of p300
0.002
Plumbagin
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.02
Plumbagin
Homo sapiens
-
recombinant full-length p300
0.0016 - 0.00974
PU139
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.00249
PU139
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.00534
PU139
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
0.00839
PU139
Homo sapiens
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 pH and temperature not specified in the publication
additional information
additional information
Homo sapiens
-
10, 25, 50 microM inhibit FLAG-tagged recombinant PCAF in vitro with an IC50 beyond 50 microM with purified human HeLa core histone as substrate
-
additional information
additional information
Homo sapiens
-
Hep-G2 hepatocarcinoma cells: with 5 microM plumbagin 50% reduction of histone H3 acetylation, with 25 microM 90% reduction, significant overall acetylation status of histones, prominent reduction in H3 and H4, immunofluorescence analysis (anti-acetylated histone H3 polyclonal antibodies) of HeLa cells (treated with deacetylase inhibitors to induce histone acetylation) confirm the inhibitory effect of plumbagin with 5 microM inhibitor, with 25 microM almost complete reduction in acetylation level
-
additional information
additional information
Mus musculus
-
significant decrease of histone acetylation in plumbagin treated mouse liver in vivo 6 h after intraperitoneal injection of 25 mg plumbagin/kg body mass
-
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evolution
-
acetyltransferases are very well conserved through evolution
evolution
-
acetyltransferases are very well conserved through evolution
evolution
histone acetyltransferase KAT8 is a member of the MYST family
evolution
histone acetyltransferase p300 is a member of the p300/CBP family
evolution
-
histone acetyltransferase p300/CBP-associated factor (PCAF) belongs to GCN5 family
evolution
tehe enzyme belongs to the p300/CBP enzyme family
evolution
-
the Arabidopsis genome contains 12 histone acetyltransferase genes
evolution
the enzyme belongs to the GCN5-family of lysine acetyltransferases
evolution
the enzyme belongs to the MYST family
evolution
-
Tip60, the 60 kDa HIV-1 Tat-interactive protein, is a key member of the MYST family of histone acetyltransferases (HATs)
evolution
-
according to the allosteric ligand type of the ACT domain, members of AAPatA family are divided into two groups, the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former exists only in Streptomyces, the latter are distributed in other actinobacteria (Pseudonocardiaceae, Micromonosporaceae, Nocardiopsaceae, and Streptosporangiaceae)
evolution
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according to the allosteric ligand type of the ACT domain, members of AAPatA family are divided into two groups, the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former exists only in Streptomyces, the latter are distributed in other actinobacteria (Pseudonocardiaceae, Micromonosporaceae, Nocardiopsaceae, and Streptosporangiaceae)
evolution
HBO1 (also known as KAT7, MYST2) is a canonical member of the MYST (MOZ, Ybf1/Sas3, Sas2 and Tip60) acetyltransferase family. HBO1 contains the MYST domain that is a highly conserved acetyltransferase domain shared by the MYST family such as MYST1 (MOF/KAT8), MYST2 (HBO1/KAT7), and MYST3 (MOZ/KAT6A). HBO1 comprises a cervical-loop structure proximity to the MYST domain that mediates the interaction with the N-terminal region (residues 31-80) of BRPF2 (also known as BRD1), for BRPF2 is a cofactor directing HBO1 binding to the histone
evolution
HBO1 (also known as KAT7, MYST2) is a canonical member of the MYST (MOZ, Ybf1/Sas3, Sas2 and Tip60) acetyltransferase family. HBO1 contains the MYST domain that is a highly conserved acetyltransferase domain shared by the MYST family such as MYST1 (MOF/KAT8), MYST2 (HBO1/KAT7), and MYST3 (MOZ/KAT6A). HBO1 comprises a cervical-loop structure proximity to the MYST domain that mediates the interaction with the N-terminal region (residues 31-80) of BRPF2 (also known as BRD1), for BRPF2 is a cofactor directing HBO1 binding to the histone
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the enzyme belongs to the components of transcription factor complexes
evolution
the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the enzyme belongs to the MYST family. The MYST family takes its name from the first identified members: (MOZ, KAT6A), Ybf2 (Sas3, KAT6), something about silencing (Sas2, KAT8) and Tat-interacting protein (Tip60, KAT5). To date, five human KATs have been identified in this family: MOZ, MOZ related factor (MORF, KAT6B), Tip60, HAT bound to ORC1 (HBO1, KAT7) and males absent on the first (MOF, KAT8 or MYST 1), the functional orthologue of yeast's Sas2. The defining feature of MYST family is the presence of the highly conserved MYST domain. MYST enzymes possess a highly-conserved acetyl-CoA-binding motif A within the catalytic domain. Additionally, some family members have also structural features in common with one another, such as chromodomains or plant homeodomain-linked zinc fingers. The members of this family utilize a double displacement (or ping-pong) catalytic mechanism. Autoacetylation is an important process in modulating the activity of MYST family members
evolution
the enzyme belongs to the MYST family. The MYST family takes its name from the first identified members: (MOZ, KAT6A), Ybf2 (Sas3, KAT6), something about silencing (Sas2, KAT8) and Tat-interacting protein (Tip60, KAT5). To date, five human KATs have been identified in this family: MOZ, MOZ related factor (MORF, KAT6B), Tip60, HAT bound to ORC1 (HBO1, KAT7) and males absent on the first (MOF, KAT8 or MYST 1), the functional orthologue of yeast's Sas2. The defining feature of MYST family is the presence of the highly conserved MYST domain. MYST enzymes possess a highly-conserved acetyl-CoA-binding motif A within the catalytic domain. Additionally, some family members have also structural features in common with one another, such as chromodomains or plant homeodomain-linked zinc fingers. The members of this family utilize a double displacement (or ping-pong) catalytic mechanism. Autoacetylation is an important process in modulating the activity of MYST family members
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the enzyme belongs to the nuclear receptors coactivators
evolution
the enzyme belongs to the nuclear receptors coactivators. Fungal enzyme Rtt109 shows low sequence similarity to members of other KAT families. It is comparable to p300 in terms of its tertiary structure, but has a different catalytic mechanism
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the enzyme TAF1/TBP belongs to the components of transcription factor complexes
evolution
the enzyme TAF1/TBP belongs to the components of transcription factor complexes
evolution
the enzyme TAF1/TBP belongs to the components of transcription factor complexes
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate
evolution
the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate. A characterizing feature of p300/CBP family is the presence of a loop, called the L1 loop, which connects an alpha-helix (alpha4) and a beta-sheet (beta5), and is part of the lysine and acetyl-CoA binding site
evolution
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate. A characterizing feature of p300/CBP family is the presence of a loop, called the L1 loop, which connects an alpha-helix (alpha4) and a beta-sheet (beta5), and is part of the lysine and acetyl-CoA binding site. Enzyme CBP is implicated in Rubinstein-Taybi syndrome and inflammation and mutated in lung, colon and ovarian carcinomas. The enzyme forms fusion proteins in acute myeloid leukemia
evolution
there are three major families of KATs grouped according to their sequence homology and domain organizations, which include the MYST family, GCN5/PCAF family, and p300/CBP family
evolution
three main histone/protein acetyltransferase (HAT) families, CBP/p300, GNAT (GCN5/PCAF) and MYST exist. GCN5 belongs to the GNAT family
evolution
three main histone/protein acetyltransferase (HAT) families, CBP/p300, GNAT (GCN5/PCAF) and MYST exist. PCAF belongs to the GNAT family
evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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according to the allosteric ligand type of the ACT domain, members of AAPatA family are divided into two groups, the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former exists only in Streptomyces, the latter are distributed in other actinobacteria (Pseudonocardiaceae, Micromonosporaceae, Nocardiopsaceae, and Streptosporangiaceae)
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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evolution
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the KATs belong to the enzyme families Gcn5 (KAT2A), PCAF (p300/CBP associated factor, KAT2B), Elp3 (KAT9), Hpa2 (KAT10), Hpa3, and Nut1. The common feature is the presence of four conserved 15-33 amino acid motifs indicated as A, B, C and D, in addition to various chromo- and bromodomains that can bind methylated or acetylated lysines, respectively. The A motif is the most conserved and contains the R/Q-X-X-G-X-G/A sequence that is essential for acetyl-CoA recognition and binding. Despite the structural similarities that characterize an enzyme family, the N- and C-terminal domains are quite different, and allow each enzyme to be specific for a particular substrate
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evolution
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the enzyme TAF1/TBP belongs to the components of transcription factor complexes
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evolution
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the enzyme belongs to the nuclear receptors coactivators. Fungal enzyme Rtt109 shows low sequence similarity to members of other KAT families. It is comparable to p300 in terms of its tertiary structure, but has a different catalytic mechanism
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evolution
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according to the allosteric ligand type of the ACT domain, members of AAPatA family are divided into two groups, the asparagine (Asn)-activated PatA and the cysteine (Cys)-activated PatA. The former exists only in Streptomyces, the latter are distributed in other actinobacteria (Pseudonocardiaceae, Micromonosporaceae, Nocardiopsaceae, and Streptosporangiaceae)
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evolution
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the enzyme belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. The GNAT superfamily of proteins is involved in many physiologically important reactions in eukaryotes and prokaryotes. PA4534 shares common characteristic structures with other GNAT family N-acetyltransferases and contains a potential substrate binding tunnel close to the bound acetyl-CoA. It also shows the characteristic features of GNAT proteins including the beta-bulge in b4 and the P-loop between beta4 and alpha3. The P-loop of PA4534 locates between beta4 and alpha3 that connects the diphosphate group of acetyl-CoA with the main chain nitrogen atoms from residues including G81, G83, A85, and R86
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malfunction
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cells lacking RTT109 have a high level of CAG/CTG repeat contractions and a twofold increase in breakage at CAG/CTG repeats
malfunction
disturbance of normal acetylation of K16 in histone H4 together with trimethylation of Lys20 in histone H4 is associated with early stages of tumor development
malfunction
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dysfunction is associated with diseases like asthma, cardiovascular disorders, diabetes, and cancer
malfunction
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dysfunction is associated with diseases like asthma, cardiovascular disorders, diabetes, and cancer
malfunction
dysfunction of histone acetyltransferases leads to several diseases including cancer, diabetes, and asthma
malfunction
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H4K16 hyperacetylation is associated with hyperexpression of the single male X chromosome in flies and, contrasting accordingly, the inactivated X chromosome in human cells is hypoacetylated at the same histone residue. HBO1 appears to function predominantly in transcriptional repression
malfunction
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HBO1 depletion reduces the rate of DNA synthesis, the amount of MCM complex bound to chromatin, and progression through S phase
malfunction
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MOZ generates fusion genes, such as MOZ-TIF2, MOZ-CBP and MOZ-p300, in acute myeloid leukemia by chromosomal translocation leading to repressed differentiation, hyper-proliferation, and self-renewal of myeloid progenitors through deregulation of MOZ-regulated target gene expression. Roles of MOZ and MOZ fusion genes in normal and malignant hematopoiesis, mechanism, overview
malfunction
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the haploinsufficient enzyme causes the Rubinstein-Taybi syndrome, a genetic disorder with cognitive dysfunction, by disrupting the control mechanism of neural precursor competency to differentiate
malfunction
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expression of mutant TgMYST-B produces no growth defect and fails to protect against DNA damage
malfunction
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overexpression of recombinant, tagged TgMYST-B reduces growth rate in vitro and confers protection from a DNA-alkylating agent. Cells overexpressing TgMYST-B have increased levels of ataxia telangiectasia mutated (ATM) kinase and phosphorylated H2AX and that TgMYST-B localizes to the ATM kinase gene. Pharmacological inhibitors of ATM kinase or KATs reverse the slow growth phenotype seen in parasites overexpressing TgMYST-B
malfunction
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aberrant histone acetylation contributes to disease
malfunction
antagonizing H4K16ac downregulation upon autophagy induction results in the promotion of cell death
malfunction
both histone H3 and H4 acetylation were increased upon GCN5 overexpression and decreased upon GCN5 knockdown
malfunction
enzyme inhibition significantly augments TRAIL-induced apoptotic sensitivity, which is accompanied by reduced levels of survivin, in Hep-G2, HLE and SK-HEP1 cells. Enzyme inhibition significantly decreases invasion of Huh7, HLE and SK-HEP1 cells. The level of matrix metallopeptidase 15 (MMP15) mRNA expression is significantly reduced, whereas the level of laminin alpha 3 (LAMA3) and secreted phosphoprotein 1 (SPP1) mRNA expression is significantly increased in Huh7 cells following exposure to enzyme inhibitor C646
malfunction
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enzyme PCAF-deficiency causes drastic decrease in mRNA levels of Bcl-6 and Pax5, and remarkable increase in that of B lymphocyte-induced maturation protein-1 (Blimp-1). In addition, PCAF-deficiency causes a remarkable decrease in acetylation levels of both H3K9 and H3K14 residues within chromatin surrounding the 5'-flanking regions of Bcl-6 and Pax5 genes in vivo
malfunction
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forced expression of PCAF inhibits the growth of hepatocellular carcinoma xenografts, upregulates histone H4 acetylation, suppresses phosphorylation of AKT, and accelerates cell apoptosis. Knockdown of PCAF represses cell apoptosis and accelerates proliferation in Hep-3B cells. Enzyme downregulation in hepatocellular carcinoma tissues is significantly correlated with tumor TNM staging and intrahepatic metastasis
malfunction
induced accumulation of the ddHAGCN5b(E703G) protein leads to a rapid arrest in parasite replication. Growth arrest is accompanied by a decrease in histone H3 acetylation at specific lysine residues as well as reduced expression of GCN5b target genes in GCN5b(E703G) parasites, which are identified using chromatin immunoprecipitation coupled with microarray hybridization
malfunction
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knockdown of GCN5 inhibits the osteogenic differentiation of and mineralization in mesenchymal stem cells. Impaired osteogenic differentiation by GCN5 knockdown is blocked by inhibition of NF-kappaB
malfunction
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loss of function of the Arabidopsis histone acetyltransferase GCN5 results in serious defects in terms of thermotolerance, and considerably impairs the transcriptional activation of heat stress-responsive genes. The expression of several key regulators such as the heat stress transcription factors HSFA2 and HSFA3, multiprotein bridging factor 1c (MBF1c) and UV-hypersensitive 6 (UVH6) is downregulated in the gcn5 mutant under heat stress compared with the wild-type. The GCN5 mutation affects H3K9 and H3K14 acetylation of HSFA3 and UVH6 genes under heat stress. Overexpression of the Triticum aestivum TaGCN5 gene restores thermotolerance in Arabidopsis gcn5 mutant plants
malfunction
PCAF deficiency reduces the in vitro inflammatory response in leukocytes and vascular cells involved in arteriogenesis. PCAF deficiency results in differential expression of 3505 genes during arteriogenesis and, more specifically, in impaired induction of multiple proinflammatory genes. Recruitment from the bone marrow of inflammatory cells, in particular proinflammatory Ly6Chi monocytes, is severely impaired in PCAF-/- mice
malfunction
small cell lung cancer cells are deficient of the histone acetyltransferase KAT6B. The depletion of KAT6B expression enhances cancer growth, while its restoration induces tumor suppressor-like features. Enzyme deletion or inhibition confers sensitivity to irinotecan, causes diminished expression of Brahma, and induces an increase in Rb phosphorylation
malfunction
the dysregulated gene expression induced by garcinol inhibition of the enzyme significantly inhibits Toxoplasma tachyzoite replication without being toxic to the human host cell. Garcinol inhibits TgGCN5b KAT activity and reduces global lysine acetylation in vivo in treated parasites, including its preferred substrate, histone H3
malfunction
abrogation of HBO1 activity caused by either RNA interference or dominant negative mutation (e.g. S57A) does not affect the recruitment of ORC, CDC6 and CDT1 to replication origins, but remarkably impairs the loading of MCMs to the origins and subsequently delays DNA replication licensing. In immune-related disease, HBO1 is upregulated in synovial fibroblasts, which are the key pathogenic factors contributing to the development and progression of rheumatoid arthritis. Protein HBZ (HTLV-1 basic zipper factor, from a human T cell leukemia virus) interacts with HBO1 during pathogenesis and inhibits its acetylation activity to reduce p53-mediated transcription activation of p21/CDKN1A and Gadd45a, and subsequently delays G2-cell cycle arrest
malfunction
abrogation of HBO1 activity caused by either RNA interference or dominant negative mutation (e.g. S57A) does not affect the recruitment of ORC, CDC6 and CDT1 to replication origins, but remarkably impairs the loading of MCMs to the origins and subsequently delays DNA replication licensing. In immune-related disease, HBO1 is upregulated in synovial fibroblasts, which are the key pathogenic factors contributing to the development and progression of rheumatoid arthritis. Protein HBZ (HTLV-1 basic zipper factor, from a human T cell leukemia virus) interacts with HBO1 during pathogenesis and inhibits its acetylation activity to reduce p53-mediated transcription activation of p21/CDKN1A and Gadd45a, and subsequently delays G2-cell cycle arrest
malfunction
acetyl-CoA levels are elevated in NuA4 mutants
malfunction
deletion of Gcn5 or PCAF do not affect Treg development or suppressive function in vitro, but do affect inducible Treg (iTreg) development, and in vivo, abrogate Treg-dependent allograft survival. Deletion of either CBP or p300 results in only a modest decrease in Treg suppressive function. Activated CD4+T cell population in mesenteric lymph nodes of PCAF-/- mice, contribution of PCAF to iTreg development. PCAF deletion in Foxp3+ Treg cells causes lethal autoimmunity
malfunction
deletion of Gcn5 or PCAF do not affect Treg development or suppressive function in vitro, but do affect inducible Treg (iTreg) development, and in vivo, abrogate Treg-dependent allograft survival. Mice lacking GCN5 show prolonged allograft survival, suggesting this HAT might be a target for epigenetic therapy in allograft recipients. Dual deletion of GCN5 and PCAF leads to decreased Treg stability and numbers in peripheral lymphoid tissues, and mice succumbed to severe autoimmunity by 3-4 weeks of life. Conditional deletion of GCN5 in the Tregs of GCN5flfFoxp3YFP-cre mice have no significant effect on T-cell numbers or their baseline level of immune activation. GCN5 deletion also decreases Teff cell functions in vivo. GCN5 deletion in Foxp3+ Treg cells causes lethal autoimmunity
malfunction
enzyme deficiency is associated with congenital malformations and embryolethality. Enzyme inhibition induces oxidative stress
malfunction
enzyme inhibition induces cellular senescence
malfunction
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GCN5 deletion differently affects the growth of two strains, i.e. W303-1A and D273-10B/A1. The defective mitochondrial phenotype is related to a marked decrease in mtDNA content, which also involves the deletion of specific regions of the molecule. W303-1A cells deleted of the GCN5 gene show a thermosensitive phenotype. The ratio of mtDNA to nuclear DNA is strongly decreased (50 times) in the W303-1A mutant cells compared to wild-type cells. This defect is not observed in the D273-10B/1A cells. The different level of mtDNA in the two gcn5DELTA strains is consistent with their different phenotypes and with the higher respiratory competence of W303-1A compared to D273-10B/A1 cells. Deletion of GCN5 differently affects fermentative and respirative growth. The dynamics of mtDNA depletion during cell duplication indicates the loss of specific regions
malfunction
GCN5 loss leads to a modest impairment in T cell development. The generation of iNKT cells, identified by TCRbeta antibody and NK1.1 or CD1d-alphaGalCer tetramer, is largely diminished in the thymus of GCN5 KO mice. This block cannot be compensated in the periphery, as indicated by a profound decrease in iNKT cell frequencies and numbers in the spleen and liver of GCN5 KO mice. Impaired iNKT cell development is unlikely due to elevated cell death, as annexin V-positive populations of iNKT cells in the thymus, spleen, and liver are indistinguishable between wild-type and GCN5 KO mice. Dramatic accumulation of iNKT cells at the stage 0 in thymus of Gcn5 knockout mice. Phenotype, overview. GCN5 knockdown inhibits EGR2 acetylation
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 HBO1 misregulation is linked to uncontrolled proliferation
malfunction
homozygous enzyme loss leads to lethal hematopoietic failure in mice at an early postnatal stage. Enzyme loss in adult mice results in dramatic hematopoietic failure
malfunction
inhibition of hARD1/NAA10 autoacetylation by K136R mutation induces the drop of KAT activity, but not NAT activity. Heat-induced disruption of hARD1/NAA10 structure also diminishes its lysine acetylation activity
malfunction
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knockdown of the enzyme inhibits differentiation of mesenchymal stem cells into osteoblast cells. The impaired osteogenic differentiation by enzyme knockdown is blocked by inhibition of nuclear factor kappaB
malfunction
loss of GCN5 in vivo does not promote metabolic remodeling in mouse skeletal muscle. Skeletal muscle gene expression of metabolic, angiogenic, and mitochondrial genes is not affected by loss of GCN5. Loss of GCN5 does not affect myosin heavy chain (MHC) composition, and markers of skeletal muscle development are unaffected by loss of GCN5. Skeletal muscle maximal respiratory capacity and succinate dehydrogenase (SDH) enzyme activity are not affected by loss of GCN5. Loss of GCN5 does not affect mitochondrial content or adaptations to endurance exercise training
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 Myst3 forms fusion proteins in acute myeloid leukemia
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 Myst4 forms fusion proteins in acute myeloid leukemia
malfunction
NuA4 mutants induce the expression of the inositol-3-phosphate synthase gene, INO1, which leads to excessive accumulation of inositol, a key metabolite used for phospholipid biosynthesis, called an Opi- phenotype. High-throughput genomic screens have identified many other mutants that derepress INO1 transcription, besides Opil mutants, and cause excessive accumulation of inositol, including mutants of the NuA4 complex (EAF1, EAF3, EAF5, EAF7, YAF9, and ESA1). NuA4 mutants exacerbate the growth defects of sec14-1ts under inositol-depleted conditions. As NuA4 mutants exhibit a derepression of INO1 and excessive inositol production, or Opi- phenotype, NuA4 mutants suppress the growth defect in sec14-1ts under inositol-depleted conditions. Lipid droplet dynamics are impaired in eaf1DELTA cells. The eaf1DELTA mutant negative genetic interaction with sec14-1ts and the decreased lipid droplet staining in eaf1D originate from defects within the fatty acid biosynthesis pathway
malfunction
oligomerization results in the loss of KAT activity
malfunction
oocyte enzyme deletion results in female infertility, with follicle development failure in the secondary and preantral follicle stages. Enzyme deletion results in abnormal heterochromatin configurations in oocytes. Granulosa cell-specific deletion of the enzyme does not affect follicle development or female fertility
malfunction
profound survival defects are observed belonging to mutants lacking the rv0998 gene. The mt-pat deletion alters carbon metabolism and redox homeostasis in hypoxia. The DELTAmt-pat deletion mutant grows normally in aerobic conditions and reaches a similar cell density as wild-type Mycobacterium tuberculosis in hypoxic vials. Unlike wild-type cells or a complemented strain, the DELTAmt-pat mutant progressively loses viability once hypoxia is achieved, consistent with the phenotype predicted by TNseq. In contrast to wild-type Mycobacterium tuberculosis, the DELTAmt-pat mutant continues to incorporate 2-[13C]-glucose into the oxidative branch of TCA under hypoxic conditions. Impaired survival of the DELTAmt-pat mutant in hypoxia indicates that preferential utilization of reductive TCA reactions is important for maintaining viability
malfunction
the AuA acetylation level decreases dramatically when ARD1 is mutated at R82 and Y122. The phosphorylation level of AuA is decreased in cells overexpressing K75R/K125R mutant
malfunction
the compaction phenotype of the yfmK deletions is partially bypassed by the hbsK41Q allele. This partial bypass may be explained by the action of more than one acetyltransferase at K41 or that YfmK acts at multiple sites. YfmK also acts at K3, K18, and K80, while YdgE may also act at K86
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the dysregulation of the enzyme activity is implicated in many human pathologies such as cancer, neurological and inflammatory disorders
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the dysregulation of the enzyme activity is implicated in many human pathologies such as cancer, neurological and inflammatory disorders. An aberrant activity of Gcn5 can lead to uncontrolled cell cycle progression
malfunction
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 the dysregulation of the enzyme activity is implicated in many human pathologies such as cancer, neurological and inflammatory disorders. PCAF knockdown blocks the growth of urothelial cancer cells and reduces their invasive ability
malfunction
-
cells lacking RTT109 have a high level of CAG/CTG repeat contractions and a twofold increase in breakage at CAG/CTG repeats
-
malfunction
-
the compaction phenotype of the yfmK deletions is partially bypassed by the hbsK41Q allele. This partial bypass may be explained by the action of more than one acetyltransferase at K41 or that YfmK acts at multiple sites. YfmK also acts at K3, K18, and K80, while YdgE may also act at K86
-
malfunction
-
NuA4 mutants induce the expression of the inositol-3-phosphate synthase gene, INO1, which leads to excessive accumulation of inositol, a key metabolite used for phospholipid biosynthesis, called an Opi- phenotype. High-throughput genomic screens have identified many other mutants that derepress INO1 transcription, besides Opil mutants, and cause excessive accumulation of inositol, including mutants of the NuA4 complex (EAF1, EAF3, EAF5, EAF7, YAF9, and ESA1). NuA4 mutants exacerbate the growth defects of sec14-1ts under inositol-depleted conditions. As NuA4 mutants exhibit a derepression of INO1 and excessive inositol production, or Opi- phenotype, NuA4 mutants suppress the growth defect in sec14-1ts under inositol-depleted conditions. Lipid droplet dynamics are impaired in eaf1DELTA cells. The eaf1DELTA mutant negative genetic interaction with sec14-1ts and the decreased lipid droplet staining in eaf1D originate from defects within the fatty acid biosynthesis pathway
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malfunction
-
acetyl-CoA levels are elevated in NuA4 mutants
-
malfunction
-
GCN5 deletion differently affects the growth of two strains, i.e. W303-1A and D273-10B/A1. The defective mitochondrial phenotype is related to a marked decrease in mtDNA content, which also involves the deletion of specific regions of the molecule. W303-1A cells deleted of the GCN5 gene show a thermosensitive phenotype. The ratio of mtDNA to nuclear DNA is strongly decreased (50 times) in the W303-1A mutant cells compared to wild-type cells. This defect is not observed in the D273-10B/1A cells. The different level of mtDNA in the two gcn5DELTA strains is consistent with their different phenotypes and with the higher respiratory competence of W303-1A compared to D273-10B/A1 cells. Deletion of GCN5 differently affects fermentative and respirative growth. The dynamics of mtDNA depletion during cell duplication indicates the loss of specific regions
-
malfunction
-
knockdown of GCN5 inhibits the osteogenic differentiation of and mineralization in mesenchymal stem cells. Impaired osteogenic differentiation by GCN5 knockdown is blocked by inhibition of NF-kappaB
-
malfunction
-
GCN5 loss leads to a modest impairment in T cell development. The generation of iNKT cells, identified by TCRbeta antibody and NK1.1 or CD1d-alphaGalCer tetramer, is largely diminished in the thymus of GCN5 KO mice. This block cannot be compensated in the periphery, as indicated by a profound decrease in iNKT cell frequencies and numbers in the spleen and liver of GCN5 KO mice. Impaired iNKT cell development is unlikely due to elevated cell death, as annexin V-positive populations of iNKT cells in the thymus, spleen, and liver are indistinguishable between wild-type and GCN5 KO mice. Dramatic accumulation of iNKT cells at the stage 0 in thymus of Gcn5 knockout mice. Phenotype, overview. GCN5 knockdown inhibits EGR2 acetylation
-
malfunction
-
profound survival defects are observed belonging to mutants lacking the rv0998 gene. The mt-pat deletion alters carbon metabolism and redox homeostasis in hypoxia. The DELTAmt-pat deletion mutant grows normally in aerobic conditions and reaches a similar cell density as wild-type Mycobacterium tuberculosis in hypoxic vials. Unlike wild-type cells or a complemented strain, the DELTAmt-pat mutant progressively loses viability once hypoxia is achieved, consistent with the phenotype predicted by TNseq. In contrast to wild-type Mycobacterium tuberculosis, the DELTAmt-pat mutant continues to incorporate 2-[13C]-glucose into the oxidative branch of TCA under hypoxic conditions. Impaired survival of the DELTAmt-pat mutant in hypoxia indicates that preferential utilization of reductive TCA reactions is important for maintaining viability
-
malfunction
-
profound survival defects are observed belonging to mutants lacking the rv0998 gene. The mt-pat deletion alters carbon metabolism and redox homeostasis in hypoxia. The DELTAmt-pat deletion mutant grows normally in aerobic conditions and reaches a similar cell density as wild-type Mycobacterium tuberculosis in hypoxic vials. Unlike wild-type cells or a complemented strain, the DELTAmt-pat mutant progressively loses viability once hypoxia is achieved, consistent with the phenotype predicted by TNseq. In contrast to wild-type Mycobacterium tuberculosis, the DELTAmt-pat mutant continues to incorporate 2-[13C]-glucose into the oxidative branch of TCA under hypoxic conditions. Impaired survival of the DELTAmt-pat mutant in hypoxia indicates that preferential utilization of reductive TCA reactions is important for maintaining viability
-
malfunction
-
the dysregulated gene expression induced by garcinol inhibition of the enzyme significantly inhibits Toxoplasma tachyzoite replication without being toxic to the human host cell. Garcinol inhibits TgGCN5b KAT activity and reduces global lysine acetylation in vivo in treated parasites, including its preferred substrate, histone H3
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malfunction
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GCN5 deletion differently affects the growth of two strains, i.e. W303-1A and D273-10B/A1. The defective mitochondrial phenotype is related to a marked decrease in mtDNA content, which also involves the deletion of specific regions of the molecule. W303-1A cells deleted of the GCN5 gene show a thermosensitive phenotype. The ratio of mtDNA to nuclear DNA is strongly decreased (50 times) in the W303-1A mutant cells compared to wild-type cells. This defect is not observed in the D273-10B/1A cells. The different level of mtDNA in the two gcn5DELTA strains is consistent with their different phenotypes and with the higher respiratory competence of W303-1A compared to D273-10B/A1 cells. Deletion of GCN5 differently affects fermentative and respirative growth. The dynamics of mtDNA depletion during cell duplication indicates the loss of specific regions
-
metabolism
-
beta-site amyloid precursor protein-cleaving enzyme 1 (BACE1) is acetylated in seven lysine residues that face the lumen of the ER and ER Golgi intermediate compartment (ERGIC)
metabolism
-
histone and non-histone protein acetylation is involved, directly and indirectly, in controlling the duration, strength and specificity of the NF-kappaB-activating signaling pathway at multiple levels. Overview of the NF-kB-signaling pathway. Different signaling pathways can interfere with one another by modulating the availability of HATs or HDACs for a particular transcription complex
metabolism
-
high mobility group domain-containing protein And-1 overexpression stabilizes Gcn5 through protein-protein interactions in vivo
metabolism
-
the ablation of Cullin4-RING E3 ubiquitin ligase CRL4 leads to the stabilization of isoform Gcn5 in cells with depleted And-1, and Cdc10-dependent transcript 2, i.e. Cdt2, serves as a substrate receptor protein of CRL4. Overexpression of Cdt2 reduces the isoform Gcn5 protein levels, and CRLCdt2 is sufficient to ubiquitinate Gcn5 both in vivo and in vitro. And-1 stabilizes Gcn5 by impairing the interaction between Gcn5 and CRLCdt2 and thereby preventing Gcn5 ubiquitination and degradation. The degradation of Gcn5 is not dependent on proliferating cell nuclear antigen
metabolism
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acetylation, which targets a broad range of histone and non-histone proteins, is a reversible mechanism and plays a critical role in eukaryotic genes activation/deactivation
metabolism
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acetylation, which targets a broad range of histone and non-histone proteins, is a reversible mechanism and plays a critical role in eukaryotic genes activation/deactivation
metabolism
alteration in the specific histone post-translational modification during autophagy affects the transcriptional regulation of autophagy-related genes and initiates a regulatory feedback loop,which serves as a key determinant of survival versus death responses upon autophagy induction
metabolism
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enzyme PCAF is involved in transactivation of Bcl-6 and Pax5 genes, resulting in down-regulation of Blimp-1 gene expression, and plays a key role in epigenetic regulation of B cell development
metabolism
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megakaryoblastic leukemia 1 (MKL1, also named MRTF-A), a myocardin-related transcription factor, and histone acetyltransferase p300 can synergistically augment the expression of atechol-O-methyltransferase COMT gene, increase the metabolic rate of estrogen, and thus reduce the proliferation of MCF-7 breast cancer cells stimulated by estrogen. Transactivation of COMT induced by MKL1 and p300 is mediated via MKL1-SRF-CArG-box signal transduction
metabolism
analysis of connections between NuA4, inositol, and Sec14, which is a phosphatidylinositol/phosphatidylcholine transfer protein. Overview of phospholipid metabolism. Sec14 (UniProt ID P24280) is an essential phospholipid-binding protein that coordinates the metabolism of phosphatidylinositol-4-phosphate with phosphatidylcholine (PC) at the Golgi to create a lipid environment necessary for trafficking events
metabolism
aurora kinase A colocalalizes with ARD1 during cell division and cell migration
metabolism
exogenous acetate and reduced expression of ACC1 decreases glucose-deprived stress granule formation
metabolism
exogenous acetate and reduced expression of ACC1 decreases glucose-deprived stress granule formation
metabolism
four KATs (CBP, PCAF, GCN5L2, HAT1) perform acetylation of histone H3 lysine 9 (H3K9ac) in multiple tissues across the torpor-arousal cycle, determination of protein levels
metabolism
HBO1 can be either ubiquitinated or act as an ubiquitin ligase. HBO1 acetyltransferase complexes and activity regulation, overview. The tumor suppressor p53, adipogenesis regulator FAD24 (factor for adipocyte differentiation 24, also called NOC3L) and cell cycle kinases CDK1, CDK2, CDK11 and PLK1 are linked to HBO1. Moreover, cell growth inhibitor Niam and homeobox protein SIX1 that potentiates the Warburg effect by interaction with HBO1 are also presented. HBO1 complexes mainly consist of accessory proteins MEAF6, ING4 or ING5, and two types of cofactors for chromatin binding: Jade-1/2/3 and BRPF1/2/3. HBO1 is associated with the key events of the cell cycle, especially in mitosis through physical interaction with PLK1 and CDK1. Acetylation and autoacetylation regulates HBO1 activity
metabolism
HBO1 can be either ubiquitinated or act as an ubiquitin ligase. HBO1 acetyltransferase complexes and activity regulation, overview. The tumor suppressor p53, adipogenesis regulator FAD24 (factor for adipocyte differentiation 24, also called NOC3L) and cell cycle kinases CDK1, CDK2, CDK11 and PLK1 are linked to HBO1. Moreover, cell growth inhibitor Niam and homeobox protein SIX1 that potentiates the Warburg effect by interaction with HBO1 are also presented. HBO1 complexes mainly consist of accessory proteins MEAF6, ING4 or ING5, and two types of cofactors for chromatin binding: Jade-1/2/3 and BRPF1/2/3. HBO1 is associated with the key events of the cell cycle, especially in mitosis through physical interaction with PLK1 and CDK1. Acetylation and autoacetylation regulates HBO1 activity
metabolism
in HeLa cells, ectopically overexpressed recombinant MYC-LC3 associates with endogenous KAT2A, but overexpressed Flag-KAT2A does not associate with SQSTM1. Gene silencing of SQSTM1 does not disrupt the association between KAT2A and LC3 in HeLa cells, suggesting that KAT2A physically interacts with LC3, and SQSTM1 is not involved in the interaction between KAT2A and LC3
metabolism
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 PCAF and Gcn5-mediated acetylation can be implicated in type 2 diabetes
metabolism
stress granule formation is a conserved cellular stress response. Elevated acetyl-CoA levels suppress the formation of glucose-deprived stress granules, decreased acetyl-CoA levels enhance stress granule formation upon glucose deprivation. NuA4 mutant cells exhibit reduced Pab1-GFP cytoplasmic foci upon glucose deprivation. Suppression of glucose-deprived stress granule formation by eaf7DELTA mutants is mediated by increased acetyl-CoA. Acc1 activity is reduced in eaf1DELTA cells
metabolism
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the enzyme regulates osteogenic differentiation of mesenchymal stem cells by inhibiting nuclear factor kappaB. The enzyme represses nuclear factor kappa B-dependent transcription and inhibits the nuclear factor kappaB signaling pathway
metabolism
two prototypical GNAT family members, GCN5 (general control nonrepressed-protein 5, lysine acetyltransferase (KAT)2a) and p300/CBP-associated factor (p300/CBP-associated factor (PCAF), Kat2b) contribute to Treg functions through partially distinct and partially overlapping mechanisms
metabolism
two prototypical GNAT family members, GCN5 (general control nonrepressed-protein 5, lysine acetyltransferase (KAT)2a) and p300/CBP-associated factor (p300/CBP-associated factor (PCAF), Kat2b) contribute to Treg functions through partially distinct and partially overlapping mechanisms. Transplants in mice lacking PCAF undergo acute allograft rejection. PCAF deletion also enhances anti-tumor immunity in immunocompetent mice. Dual deletion of GCN5 and PCAF leads to decreased Treg stability and numbers in peripheral lymphoid tissues, and mice succumbed to severe autoimmunity by 3-4 weeks of life
metabolism
-
analysis of connections between NuA4, inositol, and Sec14, which is a phosphatidylinositol/phosphatidylcholine transfer protein. Overview of phospholipid metabolism. Sec14 (UniProt ID P24280) is an essential phospholipid-binding protein that coordinates the metabolism of phosphatidylinositol-4-phosphate with phosphatidylcholine (PC) at the Golgi to create a lipid environment necessary for trafficking events
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metabolism
-
exogenous acetate and reduced expression of ACC1 decreases glucose-deprived stress granule formation
-
metabolism
-
stress granule formation is a conserved cellular stress response. Elevated acetyl-CoA levels suppress the formation of glucose-deprived stress granules, decreased acetyl-CoA levels enhance stress granule formation upon glucose deprivation. NuA4 mutant cells exhibit reduced Pab1-GFP cytoplasmic foci upon glucose deprivation. Suppression of glucose-deprived stress granule formation by eaf7DELTA mutants is mediated by increased acetyl-CoA. Acc1 activity is reduced in eaf1DELTA cells
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physiological function
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ATAC2 not only carries out an enzymatic function but also plays an architectural role in the stability of mammalian ATAC
physiological function
ATAC2 not only carries out an enzymatic function but also plays an architectural role in the stability of mammalian ATAC
physiological function
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CBP regulates neurobehavioural development, the enzyme activity and histone acetylation is required for control of neural cortical precursor competency to differentiate, regulation via environmental factors
physiological function
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Esa1 catalytic HAT activity is essential in yeast binding acetyl-CoA or lysine substrates and positively regulating the activities of NuA4 and Piccolo NuA4, Esa1 is involved in DNA damage repair
physiological function
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Esa1 mediates increased H4 acetylation and enhanced chromatin remodeling complex RSC occupancy and histone eviction in coding sequences and stimulates the rate of transcription elongation by polymerase II
physiological function
-
GCN5 has a general repressive effect on microRNAs, miRNAs, that guide sequence-specific posttranscriptional gene silencing, but is required for expression of a subset of MIRNA genes, overview
physiological function
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genome-wide increase in histone acetylation stimulates replication independently of transcription in follicle cells. Enok is essential for mushroom body development, the mushroom bodies are the sites of olfactory learning and memory and in this function equivalent to the mammalian brain. Mof is required for sex chromosome dosage compensation acting in the MSL complex
physiological function
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HBO1 histone acetylase is important for DNA replication licensing in a Cdt1-dependent manner, overview. HBO1 plays a direct role at replication origins as a coactivator of the Cdt1 licensing factor. As HBO1 is also a transcriptional coactivator, it has the potential to integrate internal and external stimuli to coordinate transcriptional responses with initiation of DNA replication. HBO1 is not required for Cdt1 association with replication origins
physiological function
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Hbo1 plays a role as chromatin factor serving as a positive regulator of DNA replication , chromatin structure plays an important role in DNA replication initiation
physiological function
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histone acetylation by the enzyme plays an integral role in the epigenetic regulation of gene expression
physiological function
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histone acetylation is one of the major epigenetic mechanisms to regulate gene expression. MOZ is essential for the generation and maintenance of hematopoietic stem cells and for the appropriate development of myeloid, erythroid and B-lineage cell progenitors. MOZ is also required for self-renewal of hematopoietic stem cells
physiological function
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histone acetyltransferases and deacetylases play critical roles in the regulation of chromatin structure and gene expression
physiological function
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histone and non-histone protein acetylation is involved, directly and indirectly, in controlling the duration, strength and specificity of the NF-kappaB-activating signaling pathway at multiple levels. Overview of the NF-kB-signaling pathway, IkappaBalpha and some members of the IKK complex have a nuclear function involving HAT and HDAC recruitment
physiological function
intrinsic HAT activity of p300 plays an important role in the transcriptional coactivation of CREB, c-Jun, c-Fos, c-Myb, p53, Stats, nuclear receptors, RelA GATA, p73, and others. The enzyme is involved in post-translational modifications of chromatin that play a key role in the regulation of gene expression, cell growth, and differentiation
physiological function
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Mst1 is essentially required for damage response and chromosome segregation, it plays essential roles in maintenance of genome stability and recovery from DNA damage
physiological function
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MYST1 plays a role in tumor suppression mechanisms, functional composition and mechanisms of MYST1-containing complexes, overviewS
physiological function
MYST1 plays a role in tumor suppression mechanisms, functional composition and mechanisms of MYST1-containing complexes, overviewS
physiological function
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p300 plays a key role in NFkappaB subunit acetylation
physiological function
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Qkf/Morf requirement in neural stem cell/neural progenitor self-renewal with an additional role in some other cell types such as osteoblasts and germ cells. Qkf in adult neurogenesis in vivo, overview
physiological function
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role for Rtt109 and H3K56 acetylation in maintaining repetitive DNA sequences in Saccharomyces cerevisiae
physiological function
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Rtt109 is important for repairing replication-associated lesions and has functions in addition to maintaining genome stability
physiological function
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Rtt109 is important for yeast model organisms to survive DNA damage and maintain genome integrity, and Rtt109 is particularly important for fungal pathogenicity
physiological function
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Sas2 is required for subtelomeric reporter transgene silencing, but also for transcriptional activity of transgenes integrated into rDNA, for transcriptional activation of a mutated HMRE silent mating type locus and for protection of euchromatin from heterochromatin spreading
physiological function
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the enzyme activity of MOZ is critical for the proliferation of hematopoietic precursors, overview
physiological function
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the SAGA complex contains the histone ubiquitin protease Ubp8 and the histone acetyltransferase Gcn5 and is responsible for efficient transcription of SAGA regulated genes such as GAL1 and ADH2
physiological function
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Tip60 plays multiple roles in chromatin remodeling processes. Tip60 is a partner of the epigenetic integration platform interplayed by UHRF1, DNMT1 and HDAC1 involved in the epigenetic code replication
physiological function
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a histone modifying complex, composed of the Lsy-12 MYST-type histone acetyltransferase, the Ing-family plant homeodomain protein Lsy-13, and plant homeodomain/bromodomain protein Lin-49, is required to first initiate and then actively maintain lateralized gene expression in the gustatory system. A combination of transcription factors, which recognize DNA in a sequence-specific manner, and a histone modifying enzyme complex are responsible for inducing and maintaining neuronal laterality. In lsy-12 mutants the normally ASER-specific gcy-5 gene is expressed bilaterally from the onset of its expression in threefold embryos
physiological function
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co-expression of histone acetyltransferase E1A binding protein p300 dramatically enhances Pax5-mediated transcriptional activation. The p300-mediated enhancement is dependent on its intrinsic histone acetyltransferase activity. Moreover, p300 interacts with the C terminus of Pax5 and acetylates multiple lysine residues within the paired box DNA-binding domain of Pax5. Mutations of lysine residues 67 and 87/89 to alanine within Pax5 abolish p300-mediated enhancement of Pax5-induced Luc-CD19 reporter expression in HEK-293 cells
physiological function
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coexpressing isoform TIP60 decreases the transcriptional activation ability of c-Myb in functional reporter assays. TIP60 binds to the c-Myb target gene c-Myc promoter in a c-Myb-dependent manner. Knockdown of isoform Tip60 expression by siRNA increases endogenous c-Myc expression. c-Myb is associated with histone deacetylases HDAC1 and HDAC2, known to interact with TIP60 and repress transcription
physiological function
enzyme is essential for asexual intraerythrocytic growth. Overexpression of the long, active or a truncated, non-active version of the protein by stable integration of the expression cassette in the parasite genome results in changes of H4 acetylation and cell cycle progression. Overexpressing parasites shows changes in sensitivity to DNA-damaging agents
physiological function
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high mobility group domain-containing protein And-1 forms a complex with both histone H3 and isoform Gcn5. Downregulation of And-1 results in Gcn5 degradation, leading to the reduction of histone H3K9 and H3K56 acetylation. And-1 overexpression stabilizes Gcn5 through protein-protein interactions in vivo. And-1 expression is increased in cancer cells in a manner correlating with increase in Gcn5 and acetylation of H3K9 and H3K56
physiological function
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histone acetyltransferase CLOCK is a component of the transcriptional complex that includes transcriptional factor TFIID, and infected cell proteins ICP4, ICP27, and ICP22. CLOCK histone acetyltransferase is a component of the viral transcriptional machinery throughout the replicative cycle of the virus and ICP27 and ICP22 initiate their involvement in viral gene expression as components of viral transcriptome
physiological function
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histone acetyltransferase Mof plays an essential role in the maintenance of embryonic stem cell self-renewal and pluripotency. Embryonic stem cells with Mof deletion lose characteristic morphology, alkaline phosphatase staining, and differentiation potential. They also have aberrant expression of the core transcription factors Nanog, Oct4, and Sox2. The phenotypes of Mof null embryonic stem cells can be partially suppressed by Nanog overexpression, supporting the idea that Mof functions as an upstream regulator of Nanog in embryonic stem cells. Mof is an integral component of the embryonic stem cell core transcriptional network and Mof primes genes for diverse developmental programs. Mof is also required for Wdr5 recruitment and histone H3K4 methylation at key regulatory loci
physiological function
isoform IDM1is a regulator of DNA demethylation. IDM1 is required for preventing DNA hypermethylation of highly homologous multicopy genes and other repetitive sequences that are normally targeted for active DNA demethylation by Repressor of Silencing 1 and related 5-methylcytosine DNA glycosylases. IDM1 binds methylated DNA at chromatin sites lacking histone H3K4 di- or trimethylation and acetylates H3 to create a chromatin environment permissible for 5-methylcytosine DNA glycosylases to function
physiological function
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MYST protein acetyltransferase activity requires active site lysine autoacetylation
physiological function
MYST protein acetyltransferase activity requires active site lysine autoacetylation
physiological function
plants homozygous for T-DNA disruption alleles of GCN5 encoding a histone acetyltransferase show diminished expression of cold-regulated genes COR during cold acclimation. H3 acetylation at COR gene promoters is stimulated upon cold acclimation in gcn5 plants as in wild type plants, but the decrease in nucleosome occupancy is diminished. Thus, GCN5 is not the enzyme responsible for histone acetylation at COR gene promoters during cold acclimation
physiological function
protein mediates establishment of leaf polarity independently of ASYMMETRIC LEAVES2 and the trans-acting small interfering RNA-related pathway. Treatment with an inhibitor of histone deacetylases causes additive polarity defects in as2-1 east1-1 mutant plants. Isoform ELO3 may be involved, independent of the HDAC pathway, in the determination of polarity
physiological function
targeted reduction of ELP3 specifically in the developing Drosophila nervous system leads to a hyperactive phenotype with increase in climbing and locomotor activities and sleep loss in the adult flies, a significant expansion in synaptic bouton number and axonal length and branching in the larval neuromuscular junction as well as the misregulation of genes involved in sleep, vesicle transport and fusion, and protein chaperone activity. Ubiquitous reduction of ELP3 results in lethality
physiological function
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transcriptional coactivator gcn5 gene replacement mutants show a mild growth deficiency. Gcn5 is required for adaptation to stresses mediated by KCl and CaCl2, calcoflour white, MnCl2 and caffeine. The histone acetyltransferase activity of Gcn5 is required for its role in stress response
physiological function
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transcriptional coactivytor gcn5 gene replacement mutants show a mild growth deficiency. Gcn5 is required for adaptation to stresses mediated by KCl and CaCl2, calcoflour white, MnCl2 and caffeine. The histone acetyltransferase activity of Gcn5 is required for its role in stress response. Gcn5-dependent KCl response genes include membrane transporter VMR1 and heat-shock-response gene SSA4. The FLO8 gene, which encodes a transcriptional regulator, is up-regulated in the mutant. During KCl stress adaptation, Gcn5 shows a tendency for redistribution from short genes to the transcribed regions of long genes
physiological function
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acetylation of histones in the promoter region is a key step in transcription initiation. histone acetyltransferase p300 promotes MKL1-mediated transactivation of catechol-O-methyltransferase gene. Histone acetyltransferase p300 is recruited to the promoters of certain cardiac and smooth muscle specific genes to enhance the transactivation activity of myocardin, which is a master regulator in cardiovascular differentiation and development
physiological function
an important role for PCAF in arteriogenesis. Enzyme PCAF modulates post-ischemic gene regulation
physiological function
autophagy is an evolutionarily conserved catabolic process involved in several physiological and pathological processes. Although primarily cytoprotective, autophagy can also contribute to cell death. The histone H4 lysine 16 acetyltransferase hMOF regulates the outcome of autophagy. Induction of autophagy by rapamycin is coupled to reduction of histone H4 lysine 16 acetylation through downregulation of the histone acetyltransferase hMOF
physiological function
Elp3 is the catalytic subunit of the well-conserved transcription elongator complex. Apicomplexa lack all other elongator subunits, suggesting that the Elp3 in these organisms plays a role independent of transcription. Enzyme TgElp3 is essential in Toxoplasma and must be positioned at the mitochondrial surface for parasite viability
physiological function
enzyme GCN5 is a lysine acetyltransferase that generally regulates gene expression, expression of GCN5 promotes cell growth and the G1/S phase transition in multiple lung cancer cell lines. The enzyme potentiates the growth of non-small cell lung cancer via promotion of E2F1, cyclin D1, and cyclin E1 expression. E2F1 associates with and recruits GCN5 to sites of DNA damage. E2F1 is required for the GCN5-mediated regulation of lung cancer cell growth and for theG1/S transition. Cyclin D1 and cyclin E1 are downstream targets of E2F1. GCN5 is enriched at the E2F1-binding site of the cyclin D1, cyclin E1, or E2F1 promoters
physiological function
enzyme GCN5b seems to be essential for Toxoplasma viability. GCN5b plays a central role in transcriptional and chromatin remodeling complexes. GCN5b has a non-redundant and indispensable role in regulating gene expression required during the Toxoplasma lytic cycle GCN5b is an essential driver of tachyzoite proliferation
physiological function
enzyme KAT6B has tumor suppressorlike properties in cancer cells and exerts its tumor-inhibitory role through a defined type of histone H3 Lys23 acetyltransferase activity
physiological function
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enzyme PCAF promotes cell apoptosis and functions as a hepatocellular carcinoma repressor through acetylation of histone H4 and inactivation of AKT signaling. Enzyme PCAF regulates acetylation of histone H4 and phosphorylation of AKT in HCC
physiological function
expression of p300, but not of CBP, is strongly correlated with the malignant character of hepatocellular carcinoma. CBP/p300 HAT activity has an important role in malignant transformation, proliferation, apoptotic sensitivity and invasion in hepatocellular carcinoma
physiological function
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GCN5 is an important histone acetyltransferase that is required for gene expression changes involved in numerous plant development pathways and responses to environmental conditions in Arabidopsis. Histone acetyltransferase GCN5 is essential for heat stress-responsive gene activation and thermotolerance in Arabidopsis thaliana
physiological function
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histone acetyltransferase PCAF is involved in transactivation of Bcl-6 and Pax5 genes in immature B cells. PCAF takes part in transcriptional activation of B cell lymphoma-6 (Bcl-6) and paired box gene 5 (Pax5), which are essential transcription factors for normal development of B cells. The enzyme regulates various epigenetic events for transcriptional regulation through alterations in the chromatin structure
physiological function
lysine acetylation is a critical post-translational modification that influences protein activity, stability, and binding properties. The acetylation of histone proteins in particular is a feature of gene expression regulation. TgGCN5b is the only nuclear GCN5-family KAT known to be required for Toxoplasma tachyzoite replication
physiological function
lysine acetyltransferase 8 is a histone acetyltransferase responsible for acetylating lysine 16 on histone H4 and plays a role in cell cycle progression as well as acetylation of the tumor suppressor protein p53
physiological function
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regulation of histone acetylation is fundamental to the utilization of eukaryotic genomes in chromatin. H4K16 acetylation is thought to affect the basic properties of the chromatin fiber. Male cells display twice the amount of H4K16 acetylation but reduced levels of several other acetylation motifs including H4K5, H4K12, and H3K14 acetylation as compared to female cells due to acetyltransferase MOF. Drosophila's histone acetylation system includes (1) the extensively studied model KATs (GCN5/PCAF, CBP/P300, MOF, HAT1, and TIP60), (2) less well characterized KATs (KAT6 [MOZ/MORF], HBO1, ELP3, TAF1, and ATAC2), (3) a mostly uncharacterized class of GCN5-related KATs (NAT6, NAT9, and NAT10), (4) N-terminal acetyltransferases suggested to also acetylate internal lysines (NAA10, NAA20, NAA30, NAA40, NAA50, and NAA60), (5) putative acetyltransferases with no recognizable direct homologue in non-Drosophilid species (CG5783 and CG12560), (6) the acetyltransferase ECO, and (7) a bifunctional enzyme containing a O-GlcNAcase activity and potentially a KAT activity (MGEA5, also known as NCOAT or OGA)
physiological function
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the enzyme GCN5 plays essential roles in various developmental processes, it has a critical function in osteogenic commitment of mesenchymal stem cells. In this role, the histone acetyltransferase activity of GCN5 is not required. Enzyme GCN5 represses nuclear factor kappa B-dependent transcription and inhibits the NF-kappaB signaling pathway. GCN5 is responsible for degradation of RelA. Acetylase activity of GCN5 is dispensable for the regulation of osteogenic differentiation of mesenchymal stem cells
physiological function
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the enzyme plays critical roles in apoptosis and DNA repair
physiological function
ARD1-mediated aurora kinase A (AuA) acetylation promotes cell proliferation and migration. ARD1-mediated AuA acetylation at K75/K125 enhances AuA kinase activity. Cells overexpressing AuA double mutant K75R/K125R display a dramatically decreased level of acetylated AuA, suggesting that these sites are critical for the acetylation of AuA by ARD1. AuA interacts with ARD1, and AuA acetylation is regulated by functional ARD1
physiological function
arrest defective 1 (ARD1), also known as N(alpha)-acetyltransferase 10 (NAA10) is originally identified as an N-terminal acetyltransferase (NAT) that catalyzes the acetylation of N-termini of newly synthesized peptides. Mammalian ARD1/NAA10 also plays a roleas lysine acetyltransferase (KAT) that posttranslationally acetylates internal lysine residues of proteins. ARD1/NAA10 is the only enzyme with both NAT (EC 2.3.1.255) and KAT (EC 2.3.1.48) activities. NATs acetylate N-terminal residues of newly synthesized proteins from ribosomes in an irreversible manner. N-terminal acetylation is known to be closely related to protein stability, interaction, and localization. lysine acetylation catalyzed by KATs is reversibly regulated by lysine deacetyltransferases (KDACs) that remove acetyl groups from lysine residues in proteins. While acetylation neutralizes the positive charge on lysine residues, deacetylation recovers it, thereby causing a change in electronic and conformational properties of proteins. Acetylation and deacetylation of lysine residues serve as the switches that turn-on and turn-off the cellular signal pathways and regulate diverse biological events. Any unbalance between lysine acetylation and deacetylation results in the improper regulation of biological processes and may cause various types of human diseases such as cancer and neurodegeneration
physiological function
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Asn is needed to regulate allosterically activity of SvePatA. Asp16 and Ser17 at the interface between beta1 and alpha1 may somehow affect the Cys binding of AmiPatA. Lys112 and Pro113 are not involved in the Asn binding of SvePatA. It is likely that the Pat enzymes are carefully regulated at the transcriptional and post-translational levels in response to changes of the intracellular signals that control the acetylation of specific proteins, which in turn mould the metabolic network. The relationship between the structure and function of SvePatA and AmiPatA showed that some amino acid residues at the interface between beta1-sheet and alpha1-helix may affect the ligand-binding activity. The archetypical acetyltransferases AAPatAs possessing GNAT and ACT domains show a novel signaling pathway for regulating the acetylation of cellular proteins. The acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in Actinobacteria
physiological function
at least one physiological function of the acetylation of HBsu at key lysine residues by lysine acetyltransferase YfmK is to regulate nucleoid compaction, analogous to the role of histone acetylation in eukaryotes. Acetylation is a regulatory component of the function of HBsu in nucleoid compaction. HBsu belongs to the highly conserved HU family of nucleoid-associated proteins (NAPs) and is essential for viability in Bacillus subtilis. In bacteria, the NAPs are largely responsible for chromosome compaction
physiological function
conserved role for Tip60, the mammalian homologue of Saccharomyces cerevisiae Esa1, in the regulation of stress granules in human breast cancer cells. Stress granule formation is a conserved cellular stress response. Tip60 affects stress granule levels in mammalian cells
physiological function
enzyme HBO1 is responsible for the bulk acetylation of histone H4 and H3K14. HBO1 functions as the core catalytic subunit in multimeric complexes established by cofactors and accessory proteins. HBO1 affords multiple functions in various processes such as DNA replication, gene transcription, protein ubiquitination, immune regulation, stem cell pluripotent and self-renewal maintenance as well as embryonic development. HBO1 functions as the core catalytic subunit in multimeric complexes established by cofactors and accessory proteins. HBO1 is reported to participate in transcriptional regulation in alternative complexes such as HBO1-SIX1 and HBO1-Niam. HBO1 encourages tissue-specific gene expression, for it participates in intragenic histone acetylation and mediated Pol II binding in regulating the expression of endothelial VEGFR-2. HBO1-mediated histone acetylation enables the accession of transcriptional factors to the chromatin and regulates the initiation of transcription. Alternatively, HBO1 complexes occupies the coding region to afford a direct role in transcriptional elongation. HBO1 might acetylate the transcriptional factors and change their protein-protein interactions. HBO1 facilitates chromatin loading of minichromosome maintenance (MCM) complexes and promotes DNA replication licensing. Loading of MCM complexes to chromatin is the final step of the prereplicative complexes assembly. Indispensable roles of HBO1 in chromosome remodeling and DNA replication, the mechanism regarding how HBO1 facilitates MCM loading and the involved protein-protein interactions is analyzed. HBO1 is required for T cell development and immune regulation. HBO1 acetyltransferase complexes and activity regulation, overview. Multiple functions of HBO1 are realized by the formation of protein complexes with different cofactors or partner proteins. The components of HBO1 acetyltransferase complexes and related downstream pathways may also contribute to the activity of HBO1 in cell proliferation. For example, Jade-2-mediated HBO1 acetylation activity enhances the expression of mechano-transductor signaling factor YAP1 to modulate cell elasticity in ovarian cancer. Besides, mutations in ING4 or ING5 destabilize the protein and contribute to tumorigenesis. HBO1 is essential for global acetylation of histone H3K4 and H4, thus the acetylation activity of HBO1 may also induce the expression of anti-cancer genes such as Brahma. In acute myeloid leukemia, HBO1 expression is suppressed associated with the decease of global H4K5 acetylation. Interestingly, a fusion of nucleoporin-98 (NUP98)-HBO1 is identified in a patient with chronic myelomonocytic leukemia (CMML). NUP98-HBO1 is sufficient to generate CMML pathogenesis through aberrant histone acetylation on the promoter of oncogene such as HOXA9
physiological function
enzyme HBO1 is responsible for the bulk acetylation of histone H4 and H3K14. HBO1 functions as the core catalytic subunit in multimeric complexes established by cofactors and accessory proteins. HBO1 affords multiple functions in various processes such as DNA replication, gene transcription, protein ubiquitination, immune regulation, stem cell pluripotent and self-renewal maintenance as well as embryonic development. HBO1 functions as the core catalytic subunit in multimeric complexes established by cofactors and accessory proteins. HBO1 is reported to participate in transcriptional regulation in alternative complexes such as HBO1-SIX1 and HBO1-Niam. HBO1 encourages tissue-specific gene expression, for it participates in intragenic histone acetylation and mediated Pol II binding in regulating the expression of endothelial VEGFR-2. HBO1-mediated histone acetylation enables the accession of transcriptional factors to the chromatin and regulates the initiation of transcription. Alternatively, HBO1 complexes occupies the coding region to afford a direct role in transcriptional elongation. HBO1 might acetylate the transcriptional factors and change their protein-protein interactions. HBO1 facilitates chromatin loading of minichromosome maintenance (MCM) complexes and promotes DNA replication licensing. Loading of MCM complexes to chromatin is the final step of the prereplicative complexes assembly. Indispensable roles of HBO1 in chromosome remodeling and DNA replication, the mechanism regarding how HBO1 facilitates MCM loading and the involved protein-protein interactions is analyzed. HBO1 is required for T cell development and immune regulation. HBO1 acetyltransferase complexes and activity regulation, overview. Multiple functions of HBO1 are realized by the formation of protein complexes with different cofactors or partner proteins. HBO1 functions in spermatogenesis
physiological function
enzyme TgGCN5b is the only nuclear GCN5 family KAT known to be required for Toxoplasma tachyzoite replication
physiological function
GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
physiological function
histone acetyltransferases (HATs) play critical roles in controlling T-regulation (Treg) development
physiological function
histone acetyltransferases (HATs) play critical roles in controlling T-regulation (Treg) development. PCAF helps protect Tregs from undergoing apoptosis upon TCR stimulation
physiological function
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in Saccharomyces cerevisiae the lysine-acetyltransferase Gcn5 (KAT2) is part of the SAGA complex and is responsible for histone acetylation widely or at specific lysines. In wild-type mitochondria the Gcn5 protein is present in the mitoplasts, suggesting a distinct mitochondrial function for Gcn5 independent from the SAGA complex and possibly another function for this protein connecting epigenetics and metabolism, role of Gcn5 as a factor involved in respiratory metabolism, overview
physiological function
KAT6A suppresses cellular senescence through the regulation of suppressors of the CDKN2A locus, a function that requires its KAT activity
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme CBP is implicated in Rubinstein-Taybi syndrome and inflammation, and forms fusion proteins in acute myeloid leukemia
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme CLOCK is a regulator of circadian rhythm
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme p300 is implicated in inflammation, esophageal squamous cell and hepatocellular carcinoma, and it forms fusion proteins in acute myeloid leukemia. The acetylase activity regulated by autoacetylation
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Enzyme SCR1 is involved in steroid-related transcription through pre-initiation complex formation stabilization. SRC1 KAT activity is primarily specific for histones H3 and H4, and is a consequence of ligand binding to steroid receptors. This is thought to be a mechanism by which steroid receptors and their co-activators enhance formation of a stable pre-initiation complex, thereby increasing transcription of the target genes
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. GCN5 is upregulated in non-small cell lung carcinoma, colon cancer, and glioma, and implicated in type 2 diabetes and AIDS. Gcn5 is essential in the activation and stabilization of the tumor suppressor p53. It acetylates peroxisome proliferator-activated receptor gamma co-activator 1alpha (PGC-1alpha), a co-activator which plays a central role in hepatic gluconeogenesis. PGC-1alpha acetylation triggers its degradation, leading to a decrease in blood and hepatic glucose output. In non-small-cell lung cancer (NSCLC), Gcn5 promotes cell proliferation by regulating the expression of cell cycle proteins cyclin D1, E1 and E2F1. In colon cancer tissues, Gcn5 overexpression is found to be dependent on both the cell cycle protein E2F1 and the oncogene c-myc
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. MYST enzymes have their acetylase activity regulated by autoacetylation. Tip60 activates the machinery for DNA repair
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. MYST enzymes have their acetylase activity regulated by autoacetylation. Tip60 activates the machinery for DNA repair. It is involved in numerous activities such as transcription, DNA damage cellular response, apoptosis and it has been reported to regulate p53 through acetylation at Lys120
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. PCAF acetylates the cyclin-dependent kinase inhibitor p27 leading to its degradation and facilitating cell cycle progression. PCAF is essential in the activation and stabilization of the tumor suppressor p53. It acetylates peroxisome proliferator-activated receptor gamma co-activator 1alpha (PGC-1alpha), a co-activator which plays a central role in hepatic gluconeogenesis. PGC-1alpha acetylation triggers its degradation, leading to a decrease in blood and hepatic glucose output. PCAF catalyzes the acetylation of the oncosuppressor protein PTEN on two lysine residues (Lys125 and Lys128), thereby promoting cell cycle blocking in the G1 phase after growth factor stimulation. A critical function of PCAF is the acetylation of connexin 43, which is linked to cardiac dystrophy. PCAF catalyzes the acetylation of the oncosuppressor protein PTEN on two lysine residues (Lys125 and Lys128), thereby promoting cell cycle blocking in the G1 phase after growth factor stimulation. PCAF is implicated in urothelial cancer, type 2 diabetes and cardiac dystrophy
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. TAF1 is a regulatory element in hormone-related transcriptional processes
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. TAF1 is a regulatory element in hormone-related transcriptional processes
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The enzyme is a regulatory element in hormone-related transcriptional processes. It is required for RNA polymerase III transcription
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein HBO1/MYST2 preferentially catalyzes the acetylation of histone H4. MYST enzymes have their acetylase activity regulated by autoacetylation. Enzyme HBO1/MYST2 is involved in regulation of DNA replication, since it interacts with proteins of the origin of replication complex (ORC1). HBO1 is involved in DNA replication
physiological function
lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MOF catalyzes the acetylation of p53 at lysine120, which helps to discriminate cell-cycle arrest and apoptotic functions. MYST enzymes have their acetylase activity regulated by autoacetylation
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MOF catalyzes the acetylation of p53 at lysine120, which helps to discriminate cell-cycle arrest and apoptotic functions. MYST enzymes have their acetylase activity regulated by autoacetylation. MYST1/MOF is associated with tumor growth of oral tongue squamous cell carcinoma
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MORF catalyzes the acetylation of histone H3 at Lys14. MYST enzymes have their acetylase activity regulated by autoacetylation
physiological function
O15516, O95251, P21675, Q15788, Q8WYB5, Q92793, Q92794, Q92830, Q92831, Q92993, Q9BQG0, Q9H7Z6, Q9H9T3, Q9UKN8, Q9Y6Q9 lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. The MYST protein MOZ catalyzes the acetylation of histone H3 at Lys14. MYST enzymes have their acetylase activity regulated by autoacetylation
physiological function
lysine acetyltransferase GCN5 is a regulator of mitochondrial biogenesis via its inhibitory action on peroxisome proliferator activated receptor-gamma coactivator-1alpha (PGC-1alpha). Specific contribution of GCN5 to skeletal muscle metabolism and mitochondrial adaptations to endurance exercise in vivo
physiological function
lysine acetyltransferases (KATs) play a crucial role in modulating the expression and activity of a wide-variety of cellular pathways and processes, and therefore, may play a role during hibernation when the cell is shifting to an energy conservative, cytoprotective state. Roles for lysine acetyltransferases during mammalian hibernation
physiological function
lysine acetyltransferases GCN5 is a transcription-related histone acetyltransferase. GCN5 is a specific lysine acetyltransferase of EGR2, a transcription factor required for CD1d-restricted invariant natural killer T (iNKT) cell development. The histone acetyltransferase GCN5 is essential for iNKT cell development during the maturation stage. GCN5-mediated acetylation positively regulated EGR2 transcriptional activity, and both genetic and pharmacological GCN5 suppression specifically inhibits the transcription of EGR2 target genes in iNKT cells, including Runx1, PLZF, IL-2Rb, and T-bet. Therefore, GCN5-mediated EGR2 acetylation is a molecular mechanism that regulates iNKT development. GCN5 has been shown to play critical roles in a variety of important biological functions including metabolic regulation, cell growth and survival, DNA damage repair, and embryonic development. Role of GCN5 in T cell immunity, overview. GCN5 is required for the development of iNKT cells in mice. GCN5 regulates the expression of genes driving iNKT development through EGR2
physiological function
N-terminal acetylation catalyzed by NATs is one of the most common protein modifications in eukaryotes, affecting about 80% human proteins. In general, NATs acetylate N-terminal residues of newly synthesized proteins from ribosomes in an irreversible manner. N-terminal acetylation is known to be closely related to protein stability, interaction, and localization. Human ARD1/NAA10 expanded its' role to lysine acetyltransferase (KAT) that post-translationally acetylates internal lysine residues of proteins. Size-exclusion analysis reveals that most recombinant hARD1/NAA10 forms oligomers. While oligomeric recombinant hARD1/NAA10 loses its ability for lysine acetylation, its monomeric form clearly exhibits lysine acetylation activity in vitro. In contrast to N-terminal acetylation, lysine acetylation catalyzed by KATs is reversibly regulated by lysine deacetyltransferases (KDACs) that remove acetyl groups from lysine residues in protein. hARD1 regulates a wide range of cellular functions, including cell cycle, apoptosis, migration, stress response, and differentiation. NAT and KAT activity might be independently regulated, relying on the interaction partners
physiological function
p300 and GCN5 are two representative lysine acetyltransferases (KATs) in mammalian cells. They possess multiple acyltransferase activities including acetylation, propionylation, and butyrylation of the epsilon-amino group of lysine residues of histones and non-histone protein substrates. The protein substrates are extensively involved in various biological events including gene expression, cell cycle, and cellular metabolism. Canonical KAT-related processes such as gene expression, DNA repair, cell cycle, and apoptosis involve both known and newly identified substrates of p300 and GCN5, overview
physiological function
protein acetyl-transferase MtPat promotes survival and alters the flux of carbon from oxidative to reductive TCA reactions. Essentiality of Mt-Pat in hypoxia, role for Mt-Pat orthologues in regulating acyl-CoA ligases. Mt-Pat orthologues function to regulate the formation of acetyl-CoA. The absence of this regulation in hypoxia results in continual flux of this metabolite into oxidative TCA reactions
physiological function
protein acetylation catalyzed by specific histone acetyltransferases (HATs) is an essential posttranslational modification (PTM) and involved in the regulation a broad spectrum of biological processes in eukaryotes
physiological function
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the activity of AmiPatA is regulated allosterically by Cys binding. It is likely that the Pat enzymes are carefully regulated at the transcriptional and post-translational levels in response to changes of the intracellular signals that control the acetylation of specific proteins, which in turn mould the metabolic network. The relationship between the structure and function of SvePatA and AmiPatA showed that some amino acid residues at the interface between beta1-sheet and alpha1-helix may affect the ligand-binding activity. The archetypical acetyltransferases AAPatAs possessing GNAT and ACT domains show a novel signaling pathway for regulating the acetylation of cellular proteins. The acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in Actinobacteria
physiological function
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the enzyme downregulates biofilm formation in Acinetobacter baumannii via polyamine acetylation
physiological function
the enzyme has an essential function in oogenesis and is essential for female fertility by regulating antioxidant gene expression. The enzyme directly regulates antioxidant gene expression in oocytes
physiological function
the enzyme is a developmental-stage-specific chromatin regulator whose activity is essential for adult but not early and midgestational murine hematopoietic maintenance. Enzyme activity is required for adult hematopoietic cell survival
physiological function
the enzyme is required for embryonic development
physiological function
the histone acetyltransferase KAT2A/GCN5 (lysine acetyltransferase 2) acetylates TUBA in vascular smooth muscle cells leading to microtubule instability and promotion of VSMC migration. Deacetylation of TUBA and perturbation of microtubule stability via selective autophagic degradation of KAT2A are essential for autophagy-promoting VSMC migration
physiological function
the lysine acetyltransferase complex NuA4 plays a role in phospholipid homeostasis. One role for NuA4 is the regulation of chromatin remodeling and gene transcription through the acetylation of histones H4 andH2A-Z, and NuA4 also targets nonhistone proteins
physiological function
the Saccharomyces cerevisiae lysine acetyltransferase complex NuA4 is required for stress granule (SG) formation upon glucose deprivation but not heat stress. The impact of NuA4 on glucose-deprived stress granule formation is partially mediated through regulation of acetyl-CoA levels via the acetyl-CoA carboxylase Acc1. Both NuA4 and the metabolite acetyl-CoA are critical signaling pathways regulating the formation of glucose-deprived stress granules. Functionally redundant roles for Eaf7 and Gcn5 in SG formation upon glucose deprivation, overview. NuA4 is required for glucose deprivation stress granule formation but does not impact processing bodies. NuA4 does not regulate the formation of stress granules through the inhibition of translation initiation or the Snf1 pathway. Eaf1 and Eaf7 are not required for the inhibition of translation initiation upon 10 minutes glucose deprivation
physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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role for Rtt109 and H3K56 acetylation in maintaining repetitive DNA sequences in Saccharomyces cerevisiae
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physiological function
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Asn is needed to regulate allosterically activity of SvePatA. Asp16 and Ser17 at the interface between beta1 and alpha1 may somehow affect the Cys binding of AmiPatA. Lys112 and Pro113 are not involved in the Asn binding of SvePatA. It is likely that the Pat enzymes are carefully regulated at the transcriptional and post-translational levels in response to changes of the intracellular signals that control the acetylation of specific proteins, which in turn mould the metabolic network. The relationship between the structure and function of SvePatA and AmiPatA showed that some amino acid residues at the interface between beta1-sheet and alpha1-helix may affect the ligand-binding activity. The archetypical acetyltransferases AAPatAs possessing GNAT and ACT domains show a novel signaling pathway for regulating the acetylation of cellular proteins. The acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in Actinobacteria
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physiological function
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at least one physiological function of the acetylation of HBsu at key lysine residues by lysine acetyltransferase YfmK is to regulate nucleoid compaction, analogous to the role of histone acetylation in eukaryotes. Acetylation is a regulatory component of the function of HBsu in nucleoid compaction. HBsu belongs to the highly conserved HU family of nucleoid-associated proteins (NAPs) and is essential for viability in Bacillus subtilis. In bacteria, the NAPs are largely responsible for chromosome compaction
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physiological function
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the lysine acetyltransferase complex NuA4 plays a role in phospholipid homeostasis. One role for NuA4 is the regulation of chromatin remodeling and gene transcription through the acetylation of histones H4 andH2A-Z, and NuA4 also targets nonhistone proteins
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physiological function
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the Saccharomyces cerevisiae lysine acetyltransferase complex NuA4 is required for stress granule (SG) formation upon glucose deprivation but not heat stress. The impact of NuA4 on glucose-deprived stress granule formation is partially mediated through regulation of acetyl-CoA levels via the acetyl-CoA carboxylase Acc1. Both NuA4 and the metabolite acetyl-CoA are critical signaling pathways regulating the formation of glucose-deprived stress granules. Functionally redundant roles for Eaf7 and Gcn5 in SG formation upon glucose deprivation, overview. NuA4 is required for glucose deprivation stress granule formation but does not impact processing bodies. NuA4 does not regulate the formation of stress granules through the inhibition of translation initiation or the Snf1 pathway. Eaf1 and Eaf7 are not required for the inhibition of translation initiation upon 10 minutes glucose deprivation
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physiological function
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Elp3 is the catalytic subunit of the well-conserved transcription elongator complex. Apicomplexa lack all other elongator subunits, suggesting that the Elp3 in these organisms plays a role independent of transcription. Enzyme TgElp3 is essential in Toxoplasma and must be positioned at the mitochondrial surface for parasite viability
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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in Saccharomyces cerevisiae the lysine-acetyltransferase Gcn5 (KAT2) is part of the SAGA complex and is responsible for histone acetylation widely or at specific lysines. In wild-type mitochondria the Gcn5 protein is present in the mitoplasts, suggesting a distinct mitochondrial function for Gcn5 independent from the SAGA complex and possibly another function for this protein connecting epigenetics and metabolism, role of Gcn5 as a factor involved in respiratory metabolism, overview
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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the enzyme GCN5 plays essential roles in various developmental processes, it has a critical function in osteogenic commitment of mesenchymal stem cells. In this role, the histone acetyltransferase activity of GCN5 is not required. Enzyme GCN5 represses nuclear factor kappa B-dependent transcription and inhibits the NF-kappaB signaling pathway. GCN5 is responsible for degradation of RelA. Acetylase activity of GCN5 is dispensable for the regulation of osteogenic differentiation of mesenchymal stem cells
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physiological function
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the enzyme activity of MOZ is critical for the proliferation of hematopoietic precursors, overview
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physiological function
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lysine acetyltransferases GCN5 is a transcription-related histone acetyltransferase. GCN5 is a specific lysine acetyltransferase of EGR2, a transcription factor required for CD1d-restricted invariant natural killer T (iNKT) cell development. The histone acetyltransferase GCN5 is essential for iNKT cell development during the maturation stage. GCN5-mediated acetylation positively regulated EGR2 transcriptional activity, and both genetic and pharmacological GCN5 suppression specifically inhibits the transcription of EGR2 target genes in iNKT cells, including Runx1, PLZF, IL-2Rb, and T-bet. Therefore, GCN5-mediated EGR2 acetylation is a molecular mechanism that regulates iNKT development. GCN5 has been shown to play critical roles in a variety of important biological functions including metabolic regulation, cell growth and survival, DNA damage repair, and embryonic development. Role of GCN5 in T cell immunity, overview. GCN5 is required for the development of iNKT cells in mice. GCN5 regulates the expression of genes driving iNKT development through EGR2
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physiological function
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lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts
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physiological function
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lysine acetylation is a post-translational modification of both histone and nonhistone proteins that is catalyzed by lysine acetyltransferases and plays a key role in numerous biological contexts. Rtt109 has a low catalytic efficiency in isolation, but it is much more active when associated with the histone chaperones Asf1 and Vps75. The two chaperones also determine substrate specificity, with the preferred substrate being H3K56 when Rtt109 is associated with Asf1, whereas H3K9 and H3K23 are acetylated when in complex with Vps75
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physiological function
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protein acetyl-transferase MtPat promotes survival and alters the flux of carbon from oxidative to reductive TCA reactions. Essentiality of Mt-Pat in hypoxia, role for Mt-Pat orthologues in regulating acyl-CoA ligases. Mt-Pat orthologues function to regulate the formation of acetyl-CoA. The absence of this regulation in hypoxia results in continual flux of this metabolite into oxidative TCA reactions
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physiological function
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protein acetyl-transferase MtPat promotes survival and alters the flux of carbon from oxidative to reductive TCA reactions. Essentiality of Mt-Pat in hypoxia, role for Mt-Pat orthologues in regulating acyl-CoA ligases. Mt-Pat orthologues function to regulate the formation of acetyl-CoA. The absence of this regulation in hypoxia results in continual flux of this metabolite into oxidative TCA reactions
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physiological function
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the activity of AmiPatA is regulated allosterically by Cys binding. It is likely that the Pat enzymes are carefully regulated at the transcriptional and post-translational levels in response to changes of the intracellular signals that control the acetylation of specific proteins, which in turn mould the metabolic network. The relationship between the structure and function of SvePatA and AmiPatA showed that some amino acid residues at the interface between beta1-sheet and alpha1-helix may affect the ligand-binding activity. The archetypical acetyltransferases AAPatAs possessing GNAT and ACT domains show a novel signaling pathway for regulating the acetylation of cellular proteins. The acetylation level of proteins may be closely correlated with intracellular concentrations of Asn and Cys in Actinobacteria
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physiological function
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lysine acetylation is a critical post-translational modification that influences protein activity, stability, and binding properties. The acetylation of histone proteins in particular is a feature of gene expression regulation. TgGCN5b is the only nuclear GCN5-family KAT known to be required for Toxoplasma tachyzoite replication
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physiological function
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GCN5-related N-acetyltransferases (GNATs) are a large and diverse group of enzymes which catalyze the transfer of an acetyl group from acetyl coenzyme A (Ac-CoA) to the amine group of a substrate. Substrates include protein N-terminus, lysine of histone tails, and other small molecules such as aminoglycoside, serotonin, and glucose-6-phosphate
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physiological function
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in Saccharomyces cerevisiae the lysine-acetyltransferase Gcn5 (KAT2) is part of the SAGA complex and is responsible for histone acetylation widely or at specific lysines. In wild-type mitochondria the Gcn5 protein is present in the mitoplasts, suggesting a distinct mitochondrial function for Gcn5 independent from the SAGA complex and possibly another function for this protein connecting epigenetics and metabolism, role of Gcn5 as a factor involved in respiratory metabolism, overview
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additional information
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development of a quantitative proteomic strategy to generate a comprehensive catalog of combinatorial histone acetylation and methylation motifs in Drosophila cells, acetylation patterns and their genesis by integrated enzyme activities, e.g. via enzymes MOF, RPD3, KAT6, NAA10, and GCN5, overview
additional information
mechanism by which GCN5b is recruited to target genes by co-purifying the enzyme with plant-like AP2-domain proteins, a subset of which function as DNA-binding transcription factors in Apicomplexa, overview
additional information
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mechanism by which GCN5b is recruited to target genes by co-purifying the enzyme with plant-like AP2-domain proteins, a subset of which function as DNA-binding transcription factors in Apicomplexa, overview
additional information
characterization of the Bacillus subtilis acetylome
additional information
in vitro-expressed full-length HBO1 exerts less acetylation activity compared to that of the separate MYST domain. The N-terminal domain may provide a regulatory switch for HBO1 activity
additional information
in vitro-expressed full-length HBO1 exerts less acetylation activity compared to that of the separate MYST domain. The N-terminal domain may provide a regulatory switch for HBO1 activity
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Gcn5 with bound acetyl-CoA (PDB ID 1z4r)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Tip60 with bound acetyl-CoA (PDB ID 2ou2)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
-
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a - mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. The p300/CBP-mediated transfer of acetyl group proceeds through a mechanism, in which there is no stable ternary complex. This catalytic mechanism consists of an initial stable binding of acetyl-CoA to the enzyme, followed by a weak and transient interaction with the histone substrate, necessary for acetyl transfer. Tertiary structure analysis of p300 with bound acetyl-CoA (PDB ID 4pzs)
additional information
NuA4 is a 13-subunit KAT complex containing the essential catalytic domain Esa1 and held together by the scaffolding protein Eaf1
additional information
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NuA4 is a 13-subunit KAT complex containing the essential catalytic domain Esa1 and held together by the scaffolding protein Eaf1
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
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screening of 544 human HAT-specific sites for acetylation by different HATs. Development the GPS 2.2 algorithm for the prediction of APC/C recognition motifs such as D-boxes and KEN-boxes proteins. The algorithm comprises two major parts, including the scoring strategy and performance improvement, method, overview
additional information
the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
additional information
the NAT activity is highest for the monomeric enzyme, about 2fold higher compared to the oligomeric enzyme and about 20% higher compared to the dimeric enzyme
additional information
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the NAT activity is highest for the monomeric enzyme, about 2fold higher compared to the oligomeric enzyme and about 20% higher compared to the dimeric enzyme
additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
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additional information
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characterization of the Bacillus subtilis acetylome
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additional information
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NuA4 is a 13-subunit KAT complex containing the essential catalytic domain Esa1 and held together by the scaffolding protein Eaf1
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additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
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additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
-
additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
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additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
-
additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
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additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis
-
additional information
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mechanism of action and structural analysis of KATs, detailed overview. All KATs are characterized by a similar tertiary structure in the central core. This structure consists of an alpha/beta fold, which is important for co-substrate binding and catalysis. Tertiary structure analysis of Rtt109 with bound acetyl-CoA (PDB ID 3qm0)
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additional information
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the enzyme contains an acetyl-CoA binding site located at the V-shaped cleft between beta4-beta5 strands created by beta-bulge on beta4. Another possible substrate binding site is identified close to the acetyl group of bound acetyl-CoA molecule. Acetyl-CoA adopts a C-shaped conformation where the adenosine diphosphate moiety is partly exposed to solvent and the acetyl group that is transferred to a substrate in a N-acetyltransferase reaction is deeply buried in the protein pointing towards a tunnel, potential substrate binding tunnel close to acetyl-CoA, overview. Structure comparisons
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