Histone deacetylase 1 through 11 (HDAC1-11) (HDAC1-11)

Histone deacetylases 1 through 11 (HDAC1-11) are a group of zinc-dependent enzymes that catalyze the removal of acetyl groups from the epsilon-amino groups of lysine residues on histones and various non-histone proteins. These enzymes are categorized into Class I (HDAC1, 2, 3, 8), Class II (HDAC4, 5, 6, 7, 9, 10), and Class IV (HDAC11), and they play a fundamental role in epigenetic regulation by promoting chromatin condensation and transcriptional repression. By altering the acetylation status of proteins, HDACs influence critical cellular processes including the cell cycle, apoptosis, and DNA repair (Source: UniProt, PubMed). In many cancers, HDACs are overexpressed or aberrantly recruited to promoters, leading to the silencing of tumor suppressor genes and contributing to oncogenesis. Consequently, HDAC inhibitors have been developed as therapeutic agents to reverse these epigenetic alterations, with several drugs already approved for the treatment of cutaneous and peripheral T-cell lymphomas and multiple myeloma (Source: FDA, StatPearls).

Other names

Zinc-dependent histone deacetylasesClassical histone deacetylasesHDAC familyLysine deacetylases

HDAC inhibitors bind to the zinc-containing catalytic site of the enzyme, preventing the removal of acetyl groups from lysine residues on histones and non-histone proteins. This leads to hyperacetylation of chromatin, which promotes an open chromatin structure (euchromatin), reactivates silenced tumor suppressor genes, and induces cell cycle arrest, differentiation, or apoptosis in malignant cells (Source: NIH/NCI, StatPearls).