InterPro domain: IPR017328

This entry represents eukaryotic type sirtuin-2 (Sir2, or silent information regulator) family of NAD-dependent deacetylases, which are nicotinamide adenine dinucleotide (NAD+)-dependent enzymes that hydrolyse one molecule of NAD+ for every lysine residue that is deacetylated [ 1 ]. The sirtuins are phylogenetically conserved in eukaryotes, prokaryotes, and archeal species. Sir2 itself deacetylates Lys-40 of alpha-tubulin, and is involved in the control of mitotic exit in the cell cycle, probably via its role in the regulation of cytoskeleton [ 2 ]. Other members of this family could function in telomeric silencing, cell cycle progression, chromosome stability, and/or as a regulator of gene expression through the modification of chromatin.

1. Diversity in the Sir2 family of protein deacetylases. J. Leukoc. Biol. 75, 939-50
2. Plasmodium falciparum Sir2 is an NAD+-dependent deacetylase and an acetyllysine-dependent and acetyllysine-independent NAD+ glycohydrolase. Biochemistry 47, 10227-39