Histone deacetylase

Histone deacetylase
Catalytic domain of human histone deacetylase 4 with bound inhibitor. PDB rendering based on 2vqj.[1]
Identifiers
EC no.3.5.1.98
CAS no.9076-57-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Histone deacetylase superfamily
Identifiers
SymbolHist_deacetyl
PfamPF00850
InterProIPR000286
SCOP21c3s / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Histone deacetylases (EC 3.5.1.98, HDAC) are a class of enzymes that remove acetyl groups (O=C-CH3) from an ε-N-acetyl lysine amino acid on both histone and non-histone proteins.[2] HDACs allow histones to wrap the DNA more tightly.[3] This is important because DNA is wrapped around histones, and DNA expression is regulated by acetylation and de-acetylation. HDAC's action is opposite to that of histone acetyltransferase. HDAC proteins are now also called lysine deacetylases (KDAC), to describe their function rather than their target, which also includes non-histone proteins.[4] In general, they suppress gene expression.[5]

  1. ^ Bottomley MJ, Lo Surdo P, Di Giovine P, Cirillo A, Scarpelli R, Ferrigno F, et al. (September 2008). "Structural and functional analysis of the human HDAC4 catalytic domain reveals a regulatory structural zinc-binding domain". The Journal of Biological Chemistry. 283 (39): 26694–26704. doi:10.1074/jbc.M803514200. PMC 3258910. PMID 18614528.
  2. ^ Seto, Edward; Yoshida, Minoru (2014-04-01). "Erasers of histone acetylation: the histone deacetylase enzymes". Cold Spring Harbor Perspectives in Biology. 6 (4): a018713. doi:10.1101/cshperspect.a018713. ISSN 1943-0264. PMC 3970420. PMID 24691964.
  3. ^ Milazzo G, Mercatelli D, Di Muzio G, Triboli L, De Rosa P, Perini G, Giorgi FM (May 2020). "Histone Deacetylases (HDACs): Evolution, Specificity, Role in Transcriptional Complexes, and Pharmacological Actionability". Genes. 11 (5): 556–604. doi:10.3390/genes11050556. PMC 7288346. PMID 32429325.
  4. ^ Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, et al. (August 2009). "Lysine acetylation targets protein complexes and co-regulates major cellular functions". Science. 325 (5942): 834–840. Bibcode:2009Sci...325..834C. doi:10.1126/science.1175371. PMID 19608861. S2CID 206520776.
  5. ^ Chen, Hong Ping; Zhao, Yu Tina; Zhao, Ting C (2015). "Histone Deacetylases and Mechanisms of Regulation of Gene Expression (Histone deacetylases in cancer)". Crit Rev Oncog. 20 (1–2): 35–47. doi:10.1615/critrevoncog.2015012997. PMC 4809735. PMID 25746103.