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The first sirtuin was identified in yeast (a lower eukaryote) and named sir2. In more complex mammals, there are seven known enzymes that act in cellular regulation, as sir2 does in yeast. These genes are designated as belonging to different classes (I-IV), depending on their amino acid sequence structure. [20]
Sirtuin 1, also known as NAD-dependent deacetylase sirtuin-1, is a protein that in humans is encoded by the SIRT1 gene. [5] [6] [7]SIRT1 stands for sirtuin (silent mating type information regulation 2 homolog) 1 (S. cerevisiae), referring to the fact that its sirtuin homolog (biological equivalent across species) in yeast (Saccharomyces cerevisiae) is Sir2.
NAD-dependent deacetylase sirtuin-3, mitochondrial also known as SIRT3 is a protein that in humans is encoded by the SIRT3 gene [sirtuin (silent mating type information regulation 2 homolog) 3 (S. cerevisiae)]. [5] [6] SIRT3 is member of the mammalian sirtuin family of proteins, which are homologs to the yeast Sir2 protein.
NAD-dependent deacetylase sirtuin 2 is an enzyme that in humans is encoded by the SIRT2 gene. [ 5 ] [ 6 ] [ 7 ] SIRT2 is an NAD+ (nicotinamide adenine dinucleotide)-dependent deacetylase. Studies of this protein have often been divergent, highlighting the dependence of pleiotropic effects of SIRT2 on cellular context.
Sirtuin 6 (SIRT6 or Sirt6) is a stress responsive protein deacetylase and mono-ADP ribosyltransferase enzyme encoded by the SIRT6 gene. [ 5 ] [ 6 ] [ 7 ] In laboratory research, SIRT6 appears to function in multiple molecular pathways related to aging, including DNA repair, telomere maintenance, glycolysis and inflammation . [ 5 ]
It was the first-discovered member of the Sirtuin protein family and it is highly conserved, with homologs found in organisms ranging from humans to bacteria [16] and archaea. [12] It interacts with a variety of protein substrates, but does not exhibit strong affinity for DNA, chromatin, or other silencer-binding factors. [12]
Sirtuin-activating compounds (STAC) are chemical compounds having an effect on sirtuins, a group of enzymes that use NAD+ to remove acetyl groups from proteins. They are caloric restriction mimetic compounds that may be helpful in treating various aging -related diseases.
The main ones are histone deacetylases (HDACs) and sirtuins (SIRT1,2,3,5). [2] Because histone proteins were the first known substrate for protein deacetylases, the latter all tend to be called HDACs of one class or another. Human protein deacetylase enzymes have been categorized into Class I (HDAC1,2,3,8); Class II (HDAC4,5,6,7,9,10),