Histone deacetylase 1, Histone deacetylase 2, Histone deacetylase 3, Histone deacetylase 10 (HDAC1, HDAC2, HDAC3, HDAC10)

Histone deacetylase 1, 2, 3, and 10 are zinc-dependent enzymes that remove acetyl groups from lysine residues on histone tails, promoting chromatin condensation and transcriptional repression. HDACs also modify various non-histone proteins, affecting cellular processes such as cell cycle progression, apoptosis, and DNA repair. While HDAC1, HDAC2, and HDAC3 belong to class I HDACs and are mostly nuclear, HDAC10 belongs to class IIb and has unique polyamine deacetylase activity. Aberrant activity or expression of these enzymes is implicated in cancer and other diseases, making them important therapeutic targets for HDAC inhibitors[2][3][4][6][7].

Other names

HDACsRPD3-like proteinsDeacetylasehistone deacetylaseclass I/II HDACs

Inhibitors bind the HDAC catalytic domain (often Zn2+-dependent), block deacetylation of histone and non-histone substrates, resulting in hyperacetylation and altered gene expression, commonly leading to cell cycle arrest, apoptosis, or differentiation in cancer cells[2][3][1]. HDAC10 is distinct in being a polyamine deacetylase, not a true histone deacetylase[4].