EC 2.3.1.48 - Histone acetyltransferase

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IntEnz Enzyme Nomenclature
EC 2.3.1.48

Names

Accepted name:
histone acetyltransferase
Other names:
histone acetokinase
histone acetylase
histone transacetylase
nucleosome-histone acetyltransferase
lysine acetyltransferase
protein lysine acetyltransferase
acetyl-CoA:histone acetyltransferase
Systematic name:
acetyl-CoA:[protein]-L-lysine acetyltransferase

Reactions

Comments:

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

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ERGO , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004402
CAS Registry Number: 9054-51-7
UniProtKB/Swiss-Prot: (150) [show] [UniProt]

References

  1. Gallwitz, D. and Sures, I.
    Histone acetylation. Purification and properties of three histone-specific acetyltransferases from rat thymus nuclei.
    Biochim. Biophys. Acta 263: 315-328 (1972). [PMID: 5031160]
  2. Makowski, A. M., Dutnall, R. N., 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: 43499-43502 (2001). [PMID: 11585814]
  3. Lee, K. K., Workman, J. L.
    Histone acetyltransferase complexes: one size doesn't fit all.
    Nat. Rev. Mol. Cell Biol. 8: 284-295 (2007). [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: E216 (2011). [PMID: 22010215]
  5. Wu, H., Moshkina, N., Min, J., Zeng, H., Joshua, J., Zhou, M. M., Plotnikov, A. N.
    Structural basis for substrate specificity and catalysis of human histone acetyltransferase 1.
    Proc. Natl. Acad. Sci. U.S.A. 109: 8925-8930 (2012). [PMID: 22615379]
  6. Das, C., Roy, S., Namjoshi, S., Malarkey, C. S., Jones, D. N., Kutateladze, T. G., Churchill, M. E., Tyler, J. K.
    Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation.
    Proc. Natl. Acad. Sci. U.S.A. 111: E1072-E1081 (2014). [PMID: 24616510]

[EC 2.3.1.48 created 1976, modified 2017]