Histone deacetylase | |||||||||
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![]() 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 | |||||||||
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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]
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