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Literature summary for 2.3.1.48 extracted from

  • Berndsen, C.E.; Albaugh, B.N.; Tan, S.; Denu, J.M.
    Catalytic mechanism of a MYST family histone acetyltransferase (2007), Biochemistry, 46, 623-629.
    View publication on PubMedView publication on EuropePMC

Protein Variants

Protein Variants Comment Organism
C304A site-directed mutagenesis, the mutant shows activity and pH-dependence similar to the wild-type enzyme Saccharomyces cerevisiae
C304S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
E338Q site-directed mutagenesis, the mutant shows 200fold reduced kcat at pH 7.5 compared to the wild-type enzyme Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetic analyses, kinetic mechanism Saccharomyces cerevisiae
0.0012
-
acetyl-CoA pH 7.5, 25°C, mutant E338Q Saccharomyces cerevisiae
0.0015
-
acetyl-CoA pH 7.5, 25°C, mutant C304A Saccharomyces cerevisiae
0.002
-
acetyl-CoA pH 7.5, 25°C, mutant C304S Saccharomyces cerevisiae
0.0025
-
acetyl-CoA pH 7.5, 25°C, wild-type enzyme Saccharomyces cerevisiae
0.135
-
piccoloNuA4 peptide pH 7.5, 25°C, mutant E338Q Saccharomyces cerevisiae
0.182
-
piccoloNuA4 peptide pH 7.5, 25°C, mutant C304S Saccharomyces cerevisiae
0.216
-
piccoloNuA4 peptide pH 7.5, 25°C, wild-type enzyme Saccharomyces cerevisiae
0.372
-
piccoloNuA4 peptide pH 7.5, 25°C, mutant C304A Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
histone + acetyl-CoA Saccharomyces cerevisiae
-
acetyl-histone + CoA
-
?
piccoloNuA4 peptide + acetyl-CoA Saccharomyces cerevisiae the peptide is part of the physiologic enzme complex, overview acetyl-piccoloNuA4 peptide + CoA
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae Q08649
-
-

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine ordered sequential catalytic mechanism of the MYST HAT with a direct-attack mechanism and direct acetyl transfer mechanism, not mediated by Cys304, within an Esa1‚acetyl-CoA‚histone ternary complex, acetyl-CoA binds first and CoA is the last product released Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
histone + acetyl-CoA
-
Saccharomyces cerevisiae acetyl-histone + CoA
-
?
histone + propionyl-CoA
-
Saccharomyces cerevisiae propionyl-histone + CoA
-
?
histone H4 + acetyl-CoA
-
Saccharomyces cerevisiae acetyl-histone H4 + CoA
-
?
additional information in the absence of histone acceptor, slow rates of enzyme autoacetylation and of CoA formation occur Saccharomyces cerevisiae ?
-
?
piccoloNuA4 peptide + acetyl-CoA the peptide is part of the physiologic enzme complex, overview Saccharomyces cerevisiae acetyl-piccoloNuA4 peptide + CoA
-
?
piccoloNuA4 peptide + propionyl-CoA
-
Saccharomyces cerevisiae propionyl-piccoloNuA4 peptide + CoA
-
?

Synonyms

Synonyms Comment Organism
Esa1
-
Saccharomyces cerevisiae
HAT
-
Saccharomyces cerevisiae
More the enzyme belongs to the MYST family histone acetyltransferase Saccharomyces cerevisiae

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Saccharomyces cerevisiae

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.0091
-
acetyl-CoA pH 7.5, 25°C, mutant E338Q Saccharomyces cerevisiae
0.14
-
acetyl-CoA pH 7.5, 25°C, mutant C304S Saccharomyces cerevisiae
0.76
-
acetyl-CoA pH 7.5, 25°C, mutant C304A Saccharomyces cerevisiae
1.6
-
acetyl-CoA pH 7.5, 25°C, wild-type enzyme Saccharomyces cerevisiae

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Saccharomyces cerevisiae

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
pH profiles of wild-type and mutant enzymes Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
Saccharomyces cerevisiae