IUBMB Enzyme Nomenclature


Accepted name: histone acetyltransferase

Reaction: acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N6-acetyl-L-lysine

Other name(s): nucleosome-histone acetyltransferase; histone acetokinase; histone acetylase; histone transacetylase; lysine acetyltransferase; protein lysine acetyltransferase; acetyl-CoA:histone acetyltransferase

Systematic name: acetyl-CoA:[protein]-L-lysine acetyltransferase

Comments: A group of enzymes acetylating histones. Several of the enzymes can also acetylate lysines in other proteins [3,4].

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9054-51-7


1. Gallwitz, D. and Sures, I. Histone acetylation. Purification and properties of three histone-specific acetyltransferases from rat thymus nuclei. Biochim. Biophys. Acta 263 (1972) 315-328. [PMID: 5031160]

2. Makowski, A.M., Dutnall, R.N. and Annunziato, A.T. Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase. J. Biol. Chem. 276 (2001) 43499-43502. [PMID: 11585814]

3. Lee, K.K. and Workman, J.L. Histone acetyltransferase complexes: one size doesn’t fit all. Nat. Rev. Mol. Cell. Biol. 8 (2007) 284-295. [PMID: 17380162]

4. Thao, S. and Escalante-Semerena, J.C. Biochemical and thermodynamic analyses of Salmonella enterica Pat, a multidomain, multimeric Nε-lysine acetyltransferase involved in carbon and energy metabolism. MBio 2 (2011) E216. [PMID: 22010215]

5. Wu, H., Moshkina, N., Min, J., Zeng, H., Joshua, J., Zhou, M.M. and Plotnikov, A.N. Structural basis for substrate specificity and catalysis of human histone acetyltransferase 1. Proc. Natl. Acad. Sci. USA 109 (2012) 8925-8930. [PMID: 22615379]

6. Das, C., Roy, S., Namjoshi, S., Malarkey, C.S., Jones, D.N., Kutateladze, T.G., Churchill, M.E. and Tyler, J.K. Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation. Proc. Natl. Acad. Sci. USA 111 (2014) E1072-E1081. [PMID: 24616510]

[EC created 1976, modified 2017]

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