Lysine-modifying enzymes

Lysine-modifying enzymes are a diverse group of proteins responsible for adding or removing chemical groups on the lysine residues of target proteins, most notably histones [1]. This class includes lysine acetyltransferases (KATs), lysine deacetylases (HDACs), lysine methyltransferases (KMTs), and lysine demethylases (KDMs) [2]. By altering the post-translational modification landscape, these enzymes play a critical role in regulating chromatin structure, gene transcription, and the function of various non-histone proteins involved in signaling and DNA repair [3]. Dysregulation of these enzymes is frequently linked to the pathogenesis of various cancers, where they can drive the expression of oncogenes or silence tumor suppressors [4]. Consequently, they have become significant therapeutic targets, with several inhibitors already approved for clinical use in oncology and many others in various stages of clinical development [5]. Beyond oncology, these enzymes are being investigated for their roles in neurodegenerative, inflammatory, and metabolic diseases [3]. The therapeutic strategy typically involves small-molecule inhibition of the enzyme's catalytic site to restore normal epigenetic patterns [5]. However, the broad biological impact of these enzymes can lead to significant side effects, necessitating the development of more selective inhibitors [2].

Other names

Protein lysine-modifying enzymesHistone-modifying enzymesLysine post-translational modification enzymes

Inhibition of enzymatic activity (acetylation, deacetylation, methylation, or demethylation) to modulate gene expression and protein function.