IntEnz

EC 2.3.1.48 - Histone acetyltransferase

IntEnz Enzyme Nomenclature
EC 2.3.1.48

Names

Reactions

• 21992
  acetyl-CoA

  acetyl-CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57288

  Formula: C23H34N7O17P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  L-lysyl-[histone]

  L-lysyl-[histone]

  GENERIC:9845

  Is ROOT: no
  ROOT compound: GENERIC:9844

  Number of residues: 1

  L-lysine residue L-lysine residue Name origin: UniProt - CHECKED (C) CHEBI:29969 Formula: C6H13N2O Charge: 1 Position: undefined ChEBI compound status: CHECKED (C)

  =

  CoA

  CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57287

  Formula: C21H32N7O16P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  N⁶-acetyl-L-lysyl-[histone]

  N(6)-acetyl-L-lysyl-[histone]

  GENERIC:11338

  Is ROOT: no
  ROOT compound: GENERIC:9844

  Number of residues: 1

  N6-acetyl-L-lysine residue N(6)-acetyl-L-lysine residue Name origin: UniProt - CHECKED (C) CHEBI:61930 Formula: C8H14N2O2 Charge: 0 Position: undefined ChEBI compound status: CHECKED (C)
• 45948 [IUBMB]
  acetyl-CoA

  acetyl-CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57288

  Formula: C23H34N7O17P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  L-lysyl-[protein]

  L-lysyl-[protein]

  GENERIC:9752

  Is ROOT: no
  ROOT compound: GENERIC:9624

  Number of residues: 1

  L-lysine residue L-lysine residue Name origin: UniProt - CHECKED (C) CHEBI:29969 Formula: C6H13N2O Charge: 1 Position: undefined ChEBI compound status: CHECKED (C)

  =

  CoA

  CoA

  Name origin: UniProt - CHECKED (C)

  CHEBI:57287

  Formula: C21H32N7O16P3S
  Charge: -4

  ChEBI compound status: CHECKED (C)

  

  +

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  N⁶-acetyl-L-lysyl-[protein]

  N(6)-acetyl-L-lysyl-[protein]

  GENERIC:10731

  Is ROOT: no
  ROOT compound: GENERIC:9624

  Number of residues: 1

  N6-acetyl-L-lysine residue N(6)-acetyl-L-lysine residue Name origin: UniProt - CHECKED (C) CHEBI:61930 Formula: C8H14N2O2 Charge: 0 Position: undefined ChEBI compound status: CHECKED (C)

Comments:

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

Links to other databases

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]