BRENDA - Enzyme Database show
show all sequences of 1.14.11.27

4-biphenylalanine- and 3-phenyltyrosine-derived hydroxamic acids as inhibitors of the JumonjiC-domain-containing histone demethylase KDM4A

Morera, L.; Roatsch, M.; Fuerst, M.C.; Hoffmann, I.; Senger, J.; Hau, M.; Franz, H.; Schuele, R.; Heinrich, M.R.; Jung, M.; ChemMedChem 11, 2063-2083 (2016)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
ascorbate
-
Homo sapiens
Cloned(Commentary)
Commentary
Organism
gene JMJD2A, recombinant expression of His-tagged KDM4A residues 1-359 in Escherichia coli strain BL21 Codon-Plus-Ril from plasmid pNIC28-Bsa4
Homo sapiens
Inhibitors
Inhibitors
Commentary
Organism
Structure
2-(2-((chroman-6-ylmethyl)amino)pyrimidin-4-yl)isonicotinic acid
-
Homo sapiens
3-(9-(dimethylamino)-N-hydroxynonanamido)propanoic acid
-
Homo sapiens
3-[hydroxy-[5-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
-
Homo sapiens
3-[hydroxy-[5-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
-
Homo sapiens
3-[hydroxy-[7-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-7-oxo-heptanoyl]amino]propanoic acid
-
Homo sapiens
3-[hydroxy-[8-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
Homo sapiens
3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
Homo sapiens
3-[hydroxy-[8-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
Homo sapiens
5-tetrazolyl acetohydrazide
-
Homo sapiens
8-(4-(2-(4-(3,5-dichlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
Homo sapiens
8-(hydroxyamino)-N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]-8-oxo-octanamide
-
Homo sapiens
methyl (2S)-2-[[4-[3-(hydroxyamino)-3-oxo-propyl]benzoyl]amino]-3-(4-phenylphenyl)propanoate
-
Homo sapiens
methyl (2S)-2-[[7-(hydroxyamino)-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
-
Homo sapiens
methyl (2S)-2-[[7-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
-
Homo sapiens
methyl (2S)-2-[[8-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
-
Homo sapiens
methyl (S)-3-(2’-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(3'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(3'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(4'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(4'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(4'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-([1,1'-biphenyl]-4-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl 3-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl 3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoate
-
Homo sapiens
additional information
4-biphenylalanine- and 3-phenyltyrosine-derived hydroxamic acids are inhibitors of the JumonjiC-domain-containing histone demethylase KDM4A, synthesis and chemical modifications on the lead structure and biochemical evaluation, structure-activity relationships, overview. For KDM4A inhibition, the best compounds are those bearing a biphenylalanine cap (both configurations) with an additional hydroxamic acid moiety, a C8 alkyl chain as spacer, and an N-alkylated warhead for the selectivity against hydroxamate-based histone deacetylases, HDACs, methyl 3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoate and 3-[hydroxy-[8-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid. Effect of inhibitors compounds methyl (2S)-2-[[7-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate, 3-[hydroxy-[7-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-7-oxo-heptanoyl]amino]propanoic acid, methyl (2S)-2-[[8-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate, and 3-[hydroxy-[8-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid on on cell proliferation of KYSE-150 and HL-60 cells
Homo sapiens
N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]heptanamide
-
Homo sapiens
N1-((3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)methyl)-N8-hydroxyoctanediamide
-
Homo sapiens
N1-(2-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
-
Homo sapiens
N1-(2-(3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
-
Homo sapiens
SW55
a hydroxamate-based histone deacetylase (HDAC) inhibitor, slight inhibition
Homo sapiens
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
-
Homo sapiens
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-phenyl-propanoate
-
Homo sapiens
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Homo sapiens
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Fe2+
required for activity
Homo sapiens
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
Homo sapiens
-
histone H3 N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
?
additional information
Homo sapiens
substrates of KDM4A are di- and trimethylated lysines 9 and 36 on histone 3 (H3K9me2/me3 and H3K36me2/me3)
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
O75164
-
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged KDM4A residues 1-359 from Escherichia coli strain BL21 Codon-Plus-Ril by metal chelating affinity chromatography to over 90% purity
Homo sapiens
Reaction
Reaction
Commentary
Organism
protein N6,N6-dimethyl-L-lysine + 2 2-oxoglutarate + 2 O2 = protein L-lysine + 2 succinate + 2 formaldehyde + 2 CO2
the catalytic mechanism, shared by all the JumonjiC-domain-containing demethylases, requires the presence of iron(II) in the active site, the co-substrate 2-oxoglutarate, and molecular oxygen. The methyl groups attached to the epsilon-amino group of lysines are oxidized to a hemiaminal, which spontaneously decomposes, releasing formaldehyde and demethylated lysine
Homo sapiens
Source Tissue
Source Tissue
Commentary
Organism
Textmining
HL-60 cell
-
Homo sapiens
-
promyelocytic leukemia cell
-
Homo sapiens
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATKAARK(me3)-SAPATGGVKKPHRYRPG-GK(biotin) + 2-oxoglutarate + O2
usage of immunodetection for assay quantification
744722
Homo sapiens
ATKAARKSAPATGGVKKPHRYRPG-GK(biotin) + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
-
744722
Homo sapiens
histone H3 N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
?
additional information
substrates of KDM4A are di- and trimethylated lysines 9 and 36 on histone 3 (H3K9me2/me3 and H3K36me2/me3)
744722
Homo sapiens
?
-
-
-
-
additional information
usage of a formaldehyde dehydrogenase (FDH) enzyme-coupled demethylase activity assay
744722
Homo sapiens
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Homo sapiens
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.003
-
pH 7.5, 37°C
Homo sapiens
3-(9-(dimethylamino)-N-hydroxynonanamido)propanoic acid
0.0068
-
pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[8-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
0.0068
-
pH 7.5, 37°C
Homo sapiens
methyl 3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoate
0.0085
-
pH 7.5, 37°C
Homo sapiens
8-(hydroxyamino)-N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]-8-oxo-octanamide
0.0136
-
pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
0.0143
-
pH 7.5, 37°C
Homo sapiens
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
0.0145
-
above, pH 7.5, 37°C
Homo sapiens
N1-((3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)methyl)-N8-hydroxyoctanediamide
0.0166
-
above, pH 7.5, 37°C
Homo sapiens
N1-(2-(3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
0.0171
-
pH 7.5, 37°C
Homo sapiens
methyl (2S)-2-[[8-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
0.0188
-
above, pH 7.5, 37°C
Homo sapiens
N1-(2-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
0.0254
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-([1,1'-biphenyl]-4-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.0258
-
pH 7.5, 37°C
Homo sapiens
methyl (2S)-2-[[4-[3-(hydroxyamino)-3-oxo-propyl]benzoyl]amino]-3-(4-phenylphenyl)propanoate
0.0276
-
pH 7.5, 37°C
Homo sapiens
methyl 3-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.029
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(3'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.037
-
pH 7.5, 37°C
Homo sapiens
2-(2-((chroman-6-ylmethyl)amino)pyrimidin-4-yl)isonicotinic acid
0.0371
-
pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[8-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
0.0466
-
pH 7.5, 37°C
Homo sapiens
5-tetrazolyl acetohydrazide
0.0476
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(3'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.0483
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(4'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.0522
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(4'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.0548
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(4'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.056
-
pH 7.5, 37°C
Homo sapiens
methyl (2S)-2-[[7-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
0.0563
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(2’-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.0606
-
pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[7-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-7-oxo-heptanoyl]amino]propanoic acid
0.0703
-
pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[5-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
0.0706
-
pH 7.5, 37°C
Homo sapiens
methyl (2S)-2-[[7-(hydroxyamino)-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
0.0939
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.2
-
above, pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[5-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
0.2
-
above, pH 7.5, 37°C
Homo sapiens
N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]heptanamide
0.201
-
pH 7.5, 37°C
Homo sapiens
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-phenyl-propanoate
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
ascorbate
-
Homo sapiens
Cloned(Commentary) (protein specific)
Commentary
Organism
gene JMJD2A, recombinant expression of His-tagged KDM4A residues 1-359 in Escherichia coli strain BL21 Codon-Plus-Ril from plasmid pNIC28-Bsa4
Homo sapiens
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
Organism
Inhibitor
Structure
0.003
-
pH 7.5, 37°C
Homo sapiens
3-(9-(dimethylamino)-N-hydroxynonanamido)propanoic acid
0.0068
-
pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[8-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
0.0068
-
pH 7.5, 37°C
Homo sapiens
methyl 3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoate
0.0085
-
pH 7.5, 37°C
Homo sapiens
8-(hydroxyamino)-N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]-8-oxo-octanamide
0.0136
-
pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
0.0143
-
pH 7.5, 37°C
Homo sapiens
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
0.0145
-
above, pH 7.5, 37°C
Homo sapiens
N1-((3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)methyl)-N8-hydroxyoctanediamide
0.0166
-
above, pH 7.5, 37°C
Homo sapiens
N1-(2-(3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
0.0171
-
pH 7.5, 37°C
Homo sapiens
methyl (2S)-2-[[8-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
0.0188
-
above, pH 7.5, 37°C
Homo sapiens
N1-(2-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
0.0254
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-([1,1'-biphenyl]-4-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.0258
-
pH 7.5, 37°C
Homo sapiens
methyl (2S)-2-[[4-[3-(hydroxyamino)-3-oxo-propyl]benzoyl]amino]-3-(4-phenylphenyl)propanoate
0.0276
-
pH 7.5, 37°C
Homo sapiens
methyl 3-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.029
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(3'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.037
-
pH 7.5, 37°C
Homo sapiens
2-(2-((chroman-6-ylmethyl)amino)pyrimidin-4-yl)isonicotinic acid
0.0371
-
pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[8-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
0.0466
-
pH 7.5, 37°C
Homo sapiens
5-tetrazolyl acetohydrazide
0.0476
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(3'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.0483
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(4'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.0522
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(4'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.0548
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(4'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.056
-
pH 7.5, 37°C
Homo sapiens
methyl (2S)-2-[[7-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
0.0563
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(2’-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.0606
-
pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[7-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-7-oxo-heptanoyl]amino]propanoic acid
0.0703
-
pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[5-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
0.0706
-
pH 7.5, 37°C
Homo sapiens
methyl (2S)-2-[[7-(hydroxyamino)-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
0.0939
-
pH 7.5, 37°C
Homo sapiens
methyl (S)-3-(6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
0.2
-
above, pH 7.5, 37°C
Homo sapiens
3-[hydroxy-[5-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
0.2
-
above, pH 7.5, 37°C
Homo sapiens
N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]heptanamide
0.201
-
pH 7.5, 37°C
Homo sapiens
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-phenyl-propanoate
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
2-(2-((chroman-6-ylmethyl)amino)pyrimidin-4-yl)isonicotinic acid
-
Homo sapiens
3-(9-(dimethylamino)-N-hydroxynonanamido)propanoic acid
-
Homo sapiens
3-[hydroxy-[5-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
-
Homo sapiens
3-[hydroxy-[5-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-5-oxo-pentanoyl]amino]propanoic acid
-
Homo sapiens
3-[hydroxy-[7-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-7-oxo-heptanoyl]amino]propanoic acid
-
Homo sapiens
3-[hydroxy-[8-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
Homo sapiens
3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
Homo sapiens
3-[hydroxy-[8-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid
-
Homo sapiens
5-tetrazolyl acetohydrazide
-
Homo sapiens
8-(4-(2-(4-(3,5-dichlorophenyl)piperidin-1-yl)ethyl)-1H-pyrazol-1-yl)pyrido[3,4-d]pyrimidin-4(3H)-one
-
Homo sapiens
8-(hydroxyamino)-N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]-8-oxo-octanamide
-
Homo sapiens
methyl (2S)-2-[[4-[3-(hydroxyamino)-3-oxo-propyl]benzoyl]amino]-3-(4-phenylphenyl)propanoate
-
Homo sapiens
methyl (2S)-2-[[7-(hydroxyamino)-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
-
Homo sapiens
methyl (2S)-2-[[7-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate
-
Homo sapiens
methyl (2S)-2-[[8-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
-
Homo sapiens
methyl (S)-3-(2’-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(3'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(3'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(4'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(4'-cyano-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(4'-fluoro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-(6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl (S)-3-([1,1'-biphenyl]-4-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl 3-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)-2-(8-(hydroxyamino)-8-oxooctanamido)propanoate
-
Homo sapiens
methyl 3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoate
-
Homo sapiens
additional information
4-biphenylalanine- and 3-phenyltyrosine-derived hydroxamic acids are inhibitors of the JumonjiC-domain-containing histone demethylase KDM4A, synthesis and chemical modifications on the lead structure and biochemical evaluation, structure-activity relationships, overview. For KDM4A inhibition, the best compounds are those bearing a biphenylalanine cap (both configurations) with an additional hydroxamic acid moiety, a C8 alkyl chain as spacer, and an N-alkylated warhead for the selectivity against hydroxamate-based histone deacetylases, HDACs, methyl 3-[hydroxy-[8-[[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoate and 3-[hydroxy-[8-[[(1R)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid. Effect of inhibitors compounds methyl (2S)-2-[[7-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-7-oxo-heptanoyl]amino]-3-(4-phenylphenyl)propanoate, 3-[hydroxy-[7-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-7-oxo-heptanoyl]amino]propanoic acid, methyl (2S)-2-[[8-[hydroxy-(3-methoxy-3-oxo-propyl)amino]-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate, and 3-[hydroxy-[8-[[(1S)-2-methoxy-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]amino]-8-oxo-octanoyl]amino]propanoic acid on on cell proliferation of KYSE-150 and HL-60 cells
Homo sapiens
N-[(1S)-2-(hydroxyamino)-2-oxo-1-[(4-phenylphenyl)methyl]ethyl]heptanamide
-
Homo sapiens
N1-((3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)methyl)-N8-hydroxyoctanediamide
-
Homo sapiens
N1-(2-(3'-chloro-6-hydroxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
-
Homo sapiens
N1-(2-(3'-chloro-6-methoxy-[1,1'-biphenyl]-3-yl)ethyl)-N8-hydroxyoctanediamide
-
Homo sapiens
SW55
a hydroxamate-based histone deacetylase (HDAC) inhibitor, slight inhibition
Homo sapiens
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-(4-phenylphenyl)propanoate
-
Homo sapiens
tert-butyl (2S)-2-[[8-(hydroxyamino)-8-oxo-octanoyl]amino]-3-phenyl-propanoate
-
Homo sapiens
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
Michaelis-Menten kinetics
Homo sapiens
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Fe2+
required for activity
Homo sapiens
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
Homo sapiens
-
histone H3 N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
?
additional information
Homo sapiens
substrates of KDM4A are di- and trimethylated lysines 9 and 36 on histone 3 (H3K9me2/me3 and H3K36me2/me3)
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged KDM4A residues 1-359 from Escherichia coli strain BL21 Codon-Plus-Ril by metal chelating affinity chromatography to over 90% purity
Homo sapiens
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
HL-60 cell
-
Homo sapiens
-
promyelocytic leukemia cell
-
Homo sapiens
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ATKAARK(me3)-SAPATGGVKKPHRYRPG-GK(biotin) + 2-oxoglutarate + O2
usage of immunodetection for assay quantification
744722
Homo sapiens
ATKAARKSAPATGGVKKPHRYRPG-GK(biotin) + succinate + formaldehyde + CO2
-
-
-
?
histone H3 N6,N6,N6-trimethyl-L-lysine36 + 2-oxoglutarate + O2
-
744722
Homo sapiens
histone H3 N6,N6-dimethyl-L-lysine36 + succinate + formaldehyde + CO2
-
-
-
?
additional information
substrates of KDM4A are di- and trimethylated lysines 9 and 36 on histone 3 (H3K9me2/me3 and H3K36me2/me3)
744722
Homo sapiens
?
-
-
-
-
additional information
usage of a formaldehyde dehydrogenase (FDH) enzyme-coupled demethylase activity assay
744722
Homo sapiens
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Homo sapiens
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Homo sapiens
General Information
General Information
Commentary
Organism
evolution
the enzme belongs to the KDM2-8 family, KDM4 (also known as JMJD2) subfamily, which includes five isoforms A-E
Homo sapiens
physiological function
histone lysine demethylase KDM4A regulates H3K9 and H3K36 methylation states
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
evolution
the enzme belongs to the KDM2-8 family, KDM4 (also known as JMJD2) subfamily, which includes five isoforms A-E
Homo sapiens
physiological function
histone lysine demethylase KDM4A regulates H3K9 and H3K36 methylation states
Homo sapiens
Other publictions for EC 1.14.11.27
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
743916
Hancock
The activity of JmjC histone ...
Homo sapiens
ACS Chem. Biol.
12
1011-1019
2017
-
1
1
-
1
-
-
1
-
1
-
-
-
1
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
1
-
-
-
-
1
-
1
-
-
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
745949
An
HistoneH3 demethylase JMJD2A ...
Homo sapiens
Oncotarget
8
49093-49109
2017
-
-
1
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
4
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
744722
Morera
4-biphenylalanine- and 3-phen ...
Homo sapiens
ChemMedChem
11
2063-2083
2016
1
-
1
-
-
-
33
1
-
1
-
2
-
2
-
-
1
1
-
2
-
-
4
-
1
-
-
-
1
-
-
-
-
-
30
1
-
1
-
-
-
-
30
33
-
1
-
1
-
2
-
-
-
1
-
2
-
-
4
-
1
-
-
-
1
-
-
-
-
2
2
-
-
-
744785
Pedersen
Continual removal of H3K9 pro ...
Mus musculus, Mus musculus C57BL/6
EMBO J.
35
1550-1564
2016
-
-
1
-
-
-
-
-
2
1
-
8
-
5
-
-
-
-
-
1
-
-
8
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
4
2
-
8
-
-
-
-
-
2
-
-
8
-
-
-
-
-
-
-
-
-
-
3
6
-
-
-
745803
Gacek-Matthews
KdmA, a histone H3 demethylas ...
Aspergillus nidulans, Aspergillus nidulans WIM126
Mol. Microbiol.
96
839-860
2015
-
-
1
-
1
-
-
-
1
1
-
4
-
3
-
-
-
-
-
-
-
-
6
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
1
-
4
-
-
-
-
-
-
-
-
6
-
1
-
-
-
-
-
-
-
-
3
3
-
-
-
744589
Ryu
Yeast histone H3 lysine 4 dem ...
Saccharomyces cerevisiae
BMC Biol.
12
75
2014
-
-
1
-
1
-
-
-
-
1
-
7
-
3
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
-
-
3
-
7
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
3
9
-
-
-
745919
Kupershmit
KDM4C (GASC1) lysine demethyl ...
Homo sapiens
Nucleic Acids Res.
42
6168-6182
2014
-
-
1
-
3
-
-
-
2
-
-
4
-
5
-
-
-
-
-
4
-
-
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
4
-
-
4
-
-
-
-
-
4
-
-
4
-
-
-
-
-
16
-
-
5
4
-
-
-
-
-
-
-
-
-
3
12
-
-
-
724709
Black
KDM4A lysine demethylase induc ...
Homo sapiens
Cell
154
541-555
2013
-
-
1
-
2
-
-
-
1
-
-
1
-
1
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
3
-
-
1
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
724813
Crona
Gene regulation by the lysine ...
Drosophila melanogaster
Dev. Biol.
373
453-463
2013
-
-
1
-
2
-
-
-
1
-
-
1
-
3
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
724815
Ishimura
Jmjd5, an H3K36me2 histone dem ...
Mus musculus
Development
139
749-759
2012
-
-
1
-
2
-
-
-
1
-
-
1
-
3
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
-
-
-
-
4
4
-
-
-
725960
Del Rizzo
Crystal structure and function ...
Homo sapiens
Mol. Cell. Biol.
32
4044-4052
2012
-
-
1
1
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
1
-
-
-
1
-
-
-
-
3
3
-
-
-
726260
Pan
The histone demethylase Jhdm1a ...
Homo sapiens, Mus musculus, Mus musculus C57/BL6J
PLoS Genet.
8
e1002761
2012
-
-
2
-
3
-
-
-
-
-
-
6
-
62
-
-
-
-
-
3
-
-
10
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
3
-
-
-
-
-
-
-
-
6
-
-
-
-
-
3
-
-
10
-
-
-
-
-
-
-
-
-
-
5
5
-
-
-
726301
Lin
HP1a targets the Drosophila KD ...
Drosophila melanogaster
PLoS ONE
7
e39758
2012
1
-
1
-
2
-
-
-
1
-
-
1
-
4
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
712996
Peng
Molecular characterization of ...
Sus scrofa
Mol. Biol. Rep.
38
4697-4704
2011
-
-
1
-
-
-
-
-
-
-
-
-
-
4
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
724651
He
KDM2b/JHDM1b, an H3K36me2-spec ...
Homo sapiens
Blood
117
3869-3880
2011
-
-
-
-
1
-
-
-
1
-
-
1
-
2
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
3
3
-
-
-
725450
Hillringhaus
Structural and evolutionary ba ...
Homo sapiens
J. Biol. Chem.
286
41616-41625
2011
-
-
1
1
-
-
-
-
1
1
-
5
-
6
-
-
1
-
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
1
-
-
-
-
-
-
3
3
-
5
-
-
-
3
-
-
-
-
12
-
-
-
-
-
-
-
-
-
-
2
6
-
-
-
726071
Liang
The histone H3K36 demethylase ...
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4742
Nucleic Acids Res.
39
4151-4165
2011
-
-
1
-
1
1
1
-
2
-
-
6
-
24
-
1
-
-
-
-
-
-
6
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
1
1
-
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-
2
-
-
6
-
-
1
-
-
-
-
-
6
-
1
-
-
-
1
-
-
-
2
4
4
2
-
-
726379
Fnu
Methylation of histone H3 lysi ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
108
540-545
2011
-
-
-
-
-
-
-
-
1
-
-
1
-
2
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
711153
Chang
Crystal structure of the catal ...
Saccharomyces cerevisiae
Biochem. J.
433
295-302
2010
-
-
-
1
-
-
-
1
-
1
-
4
-
3
-
-
-
-
-
-
-
-
7
1
1
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
1
-
4
-
-
-
-
-
-
-
-
7
1
1
-
-
-
1
-
-
-
-
1
1
-
-
-
711823
Strobl-Mazzulla
Histone demethylase JmjD2A reg ...
Gallus gallus
Dev. Cell
19
460-468
2010
-
-
1
-
1
-
-
-
1
-
-
2
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
1
-
-
2
-
-
-
-
-
1
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
696434
Marmorstein
Histone modifying enzymes: str ...
Homo sapiens
Biochim. Biophys. Acta
1789
58-68
2009
-
-
-
1
1
-
2
-
-
1
-
3
-
1
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
2
-
-
-
1
-
3
-
-
-
-
-
-
-
-
5
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
697140
Li
Alterations of histone modific ...
Homo sapiens
Carcinogenesis
30
1243-1251
2009
1
-
1
-
-
-
1
-
-
1
-
1
-
2
-
-
-
-
-
4
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
-
1
-
1
-
-
-
-
-
4
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
701212
Lan
Epigenetic regulation: methyla ...
Drosophila melanogaster
Sci. China C Life Sci.
52
311-322
2009
1
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
689255
Lloret-Llinares
Characterization of Drosophila ...
Drosophila melanogaster
Nucleic Acids Res.
36
2852-2863
2008
-
-
1
-
-
-
-
-
1
1
-
4
-
5
-
-
-
-
-
-
-
-
9
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
1
-
4
-
-
-
-
-
-
-
-
9
1
-
-
-
-
-
-
-
-
1
1
1
1
-
-
689797
Pfau
Members of a family of JmjC do ...
Rattus norvegicus
Proc. Natl. Acad. Sci. USA
105
1907-1912
2008
-
-
1
-
1
-
-
-
-
-
-
1
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
698109
Lagarou
dKDM2 couples histone H2A ubiq ...
Drosophila melanogaster
Genes Dev.
22
2799-2810
2008
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
2
2
-
-
-
698354
Cui
Histone lysine methyltransfera ...
Plasmodium falciparum
Int. J. Parasitol.
38
1083-1097
2008
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
700162
Polytarchou
The JmjC domain histone demeth ...
Mus musculus, Mus musculus C57BL/6
Mol. Cell. Biol.
28
7451-7464
2008
-
-
1
-
1
-
-
-
-
-
-
-
-
140
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
700202
Wallrath
Stimulating conversations betw ...
Drosophila melanogaster
Mol. Cell
32
601-602
2008
1
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
700209
Lin
Heterochromatin protein 1a sti ...
Drosophila melanogaster
Mol. Cell
32
696-706
2008
2
-
1
-
2
-
-
-
1
1
-
2
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
2
-
1
-
-
2
-
-
-
-
-
1
1
-
2
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
700374
He
The H3K36 demethylase Jhdm1b/K ...
Mus musculus
Nat. Struct. Mol. Biol.
15
1169-1175
2008
-
-
1
-
1
-
-
-
-
-
-
2
-
2
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
1
1
1
1
-
-
687571
Kim
Two Saccharomyces cerevisiae J ...
Saccharomyces cerevisiae
J. Biol. Chem.
282
20827-20835
2007
-
-
-
-
1
-
-
-
-
-
-
3
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
688966
Fang
The Saccharomyces cerevisiae h ...
Saccharomyces cerevisiae
Mol. Cell. Biol.
27
5055-5065
2007
1
-
1
-
4
-
-
-
-
1
2
-
-
2
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
-
4
-
-
-
-
-
-
1
2
-
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
689144
Couture
Specificity and mechanism of J ...
Homo sapiens
Nat. Struct. Mol. Biol.
14
689-695
2007
-
-
1
1
1
-
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
1
1
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
689151
Ng
Crystal structures of histone ...
Homo sapiens
Nature
448
87-91
2007
-
-
-
1
-
-
-
-
-
1
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
689746
Chen
Structural basis of the recogn ...
Homo sapiens
Proc. Natl. Acad. Sci. USA
104
10818-10823
2007
-
-
-
1
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
662947
Tsukada
Histone demethylation by a fam ...
Homo sapiens, Saccharomyces cerevisiae
Nature
439
811-816
2006
1
-
-
-
2
-
-
-
1
1
-
-
-
4
-
-
1
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
-
1
1
-
-
-
-
-
1
-
1
-
-
4
-
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-