IntEnz

EC 3.5.1.98 - Histone deacetylase

IntEnz Enzyme Nomenclature
EC 3.5.1.98

Names

Reaction

• 58196 [IUBMB]
  H₂O

  H2O

  Name origin: UniProt - CHECKED (C)

  CHEBI:15377

  Formula: H2O
  Charge: 0

  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)

  =

  acetate

  acetate

  Name origin: UniProt - CHECKED (C)

  CHEBI:30089

  Formula: C2H3O2
  Charge: -1

  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)

Comments:

A class of enzymes that remove acetyl groups from N⁶-acetyl-lysine residues on a histone. The reaction of this enzyme is opposite to that of EC 2.3.1.48, histone acetyltransferase. Histone deacetylases (HDACs) can be organized into three classes, HDAC1, HDAC2 and HDAC3, depending on sequence similarity and domain organization. Histone acetylation plays an important role in regulation of gene expression. In eukaryotes, HDACs play a key role in the regulation of transcription and cell proliferation [4]. May be identical to EC 3.5.1.17, acyl-lysine deacylase.

Links to other databases

References

1. Krieger, D.E., Levine, R., Merrifield, R.B., Vidali, G. and Allfrey, V.G.
   Chemical studies of histone acetylation. Substrate specificity of a histone deacetylase from calf thymus nuclei.
   J. Biol. Chem. 249: 332-334 (1974). [PMID: 4855628]
2. Sanchez del Pino, M.M., Lopez-Rodas, G., Sendra, R. and Tordera, V.
   Properties of the yeast nuclear histone deacetylase.
   Biochem. J. 303: 723-729 (1994). [PMID: 7980438]
3. Ouaissi, M. and Ouaissi, A.
   Histone deacetylase enzymes as potential drug targets in cancer and parasitic diseases.
   J. Biomed. Biotechnol. 2006: 13474 (2006). [PMID: 16883049]
4. Song, Y.M., Kim, Y.S., Kim, D., Lee, D.S. and Kwon, H.J.
   Cloning, expression, and biochemical characterization of a new histone deacetylase-like protein from Thermus caldophilus GK24.
   Biochem. Biophys. Res. Commun. 361: 55-61 (2007). [PMID: 17632079]
5. Finnin, M.S., Donigian, J.R., Cohen, A., Richon, V.M., Rifkind, R.A., Marks, P.A., Breslow, R. and Pavletich, N.P.
   Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors.
   Nature 401: 188-193 (1999). [PMID: 10490031]
6. Phiel, C.J., Zhang, F., Huang, E.Y., Guenther, M.G., Lazar, M.A. and Klein, P.S.
   Histone deacetylase is a direct target of valproic acid, a potent anticonvulsant, mood stabilizer, and teratogen.
   J. Biol. Chem. 276: 36734-36741 (2001). [PMID: 11473107]
7. de Ruijter, A.J.M., van Gennip, A.H., Caron, H.N., Kemp, S. and van Kuilenburg, A.B.P.
   Histone deacetylases (HDACs): characterization of the classical HDAC family.
   Biochem. J. 370: 737-749 (2003). [PMID: 12429021]

[EC 3.5.1.98 created 2008]