Back Histona desacetilasa Catalan Histon deacetyltransferase Danish Histon-Deacetylasen German Histona deacetilasa Spanish هیستون داستیلاز Persian Histone désacétylase French Histona desacetilase Galician Hiszton-deacetiláz Hungarian ヒストン脱アセチル化酵素 Japanese 히스톤 탈아세틸화효소 Korean
| 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 | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| Histone deacetylase superfamily | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | Hist_deacetyl | ||||||||
| Pfam | PF00850 | ||||||||
| InterPro | IPR000286 | ||||||||
| SCOP2 | 1c3s / SCOPe / SUPFAM | ||||||||
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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]
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
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