Sirtuin family protein deacetylase (SIRT (or SIRT1–SIRT7 for specific isoforms))

The sirtuin family comprises NAD+-dependent protein deacetylases that remove acetyl groups from lysine residues on both histone and non-histone proteins. This enzymatic action regulates chromatin structure and gene expression by promoting tighter DNA packaging through histone modification. There are seven mammalian sirtuins (SIRT1–SIRT7), each with distinct subcellular localizations—nuclear (SIRT1, SIRT6, SIRT7), cytosolic (SIRT2), mitochondrial (SIRT3, SIRT4, SIRT5)—and specialized functions. They play critical roles in regulating cellular processes such as aging/longevity, apoptosis resistance/survival signaling pathways, metabolic adaptation during caloric restriction or stress conditions, oxidative stress response mechanisms, inflammation control via immune cell signaling modulation,[1][2] and epigenetic silencing at specific genomic loci.[3] Dysregulation is implicated in cancer progression/metastasis,[4] neurodegenerative diseases like Alzheimer’s/Parkinson’s,[2] cardiovascular pathologies,[4] chronic inflammatory states,[1] among others. Note: The query refers to an activity rather unfortunate than a single molecular target. For structured data purposes it is recommended to use the canonical name for one member—for example “NAD-dependent protein deacetylase sirtuin 1” (“SIRT1”)—when referring specifically to drug targets.[4]

Other names

SirtuinsSir2-like proteinsSilent information regulator 2 homologsNAD-dependent deacetylases

Inhibition or activation of NAD+-dependent deacetylation activity on histones and transcription factors; Modulation of chromatin structure and gene silencing via removal of acetyl groups from lysine residues