Histone deacetylase-like amidohydrolase (HDAH)

Histone deacetylase-like amidohydrolase is a bacterial homologue of eukaryotic histone deacetylases (HDACs), characterized by its ability to remove acetyl groups from epsilon-acetylated lysine residues on histones and other proteins, thereby regulating gene expression through epigenetic modification[1][3][6]. The enzyme features a canonical HDAC fold, contains a catalytic zinc ion, and exhibits significant structural and functional similarity to human class II HDACs[1][3]. HDAH accepts acetylated proteins as substrates and is effectively inhibited by HDAC inhibitors such as suberoylanilide hydroxamic acid and cyclopentylpropionyl hydroxamic acid[1][2][5]. These inhibitors are relevant in cancer therapy, as aberrant HDAC activity is implicated in oncogenesis and other diseases[1][3]. The enzyme plays a critical role in bacterial gene regulation, and structural studies of HDAH have informed the design of therapeutic HDAC inhibitors for humans[1][2][3][6].

Other names

HDAHBacterial histone deacetylase homologFB188 HDAH

Inhibitors bind to the catalytic zinc ion and block the deacetylation of lysine residues on histones and other proteins, altering chromatin structure and transcriptional activity