NAD-dependent deacetylase sirtuin-2 is an enzyme that in humans is encoded by the SIRT2 gene. This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Several transcript variants are resulted from alternative splicing of this gene. [provided by RefSeq].
Silent information regulator (Sir2)-like family deacetylases (also known as sirtuins) are a group of enzymes closely related to histone deacetylases. These enzymes can be found in the cytoplasm, mitochondria or nucleus and are ubiquitously expressed. Sir2-like family deacetylases catalyze the removal of acetyl groups from lysine residues in histones and non-histone proteins, which is coupled to NAD+ hydrolysis. In general, sirtuins do not act autonomously but as components of large multiprotein complexes, such as pRb-E2F and mSin3A, that mediate important transcription regulatory pathways. Sirtuins have a role in regulation of transcription and apoptosis leading to substantial interest in inhibitors of these enzymes as possible antineoplastic agents. In addition, Sir2-like family deacteylases are involved in the normal ageing process through their role in resistance to cellular stress.