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Literature summary 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

EC Number Protein Variants Comment Organism
2.3.1.48 C304A site-directed mutagenesis, the mutant shows activity and pH-dependence similar to the wild-type enzyme Saccharomyces cerevisiae
2.3.1.48 C304S site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Saccharomyces cerevisiae
2.3.1.48 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.48 additional information
-
 additional information steady-state kinetic analyses, kinetic mechanism Saccharomyces cerevisiae
2.3.1.48 0.0012
-
 acetyl-CoA pH 7.5, 25°C, mutant E338Q Saccharomyces cerevisiae
2.3.1.48 0.0015
-
 acetyl-CoA pH 7.5, 25°C, mutant C304A Saccharomyces cerevisiae
2.3.1.48 0.002
-
 acetyl-CoA pH 7.5, 25°C, mutant C304S Saccharomyces cerevisiae
2.3.1.48 0.0025
-
 acetyl-CoA pH 7.5, 25°C, wild-type enzyme Saccharomyces cerevisiae
2.3.1.48 0.135
-
 piccoloNuA4 peptide pH 7.5, 25°C, mutant E338Q Saccharomyces cerevisiae
2.3.1.48 0.182
-
 piccoloNuA4 peptide pH 7.5, 25°C, mutant C304S Saccharomyces cerevisiae
2.3.1.48 0.216
-
 piccoloNuA4 peptide pH 7.5, 25°C, wild-type enzyme Saccharomyces cerevisiae
2.3.1.48 0.372
-
 piccoloNuA4 peptide pH 7.5, 25°C, mutant C304A Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.48 Saccharomyces cerevisiae Q08649
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.48 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
a

Substrates and Products (Substrate)

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

Synonyms

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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.3.1.48 25
-
 assay at Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.3.1.48 0.0091
-
 acetyl-CoA pH 7.5, 25°C, mutant E338Q Saccharomyces cerevisiae
2.3.1.48 0.14
-
 acetyl-CoA pH 7.5, 25°C, mutant C304S Saccharomyces cerevisiae
2.3.1.48 0.76
-
 acetyl-CoA pH 7.5, 25°C, mutant C304A Saccharomyces cerevisiae
2.3.1.48 1.6
-
 acetyl-CoA pH 7.5, 25°C, wild-type enzyme Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.3.1.48 7.5
-
 assay at Saccharomyces cerevisiae

pH Range

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

Cofactor

EC Number Cofactor Comment Organism Structure
2.3.1.48 acetyl-CoA
-
 Saccharomyces cerevisiae