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Sirtuin. Sirtuins are a family of signaling proteins involved in metabolic regulation. [ 2][ 3] They are ancient in animal evolution and appear to possess a highly conserved structure throughout all kingdoms of life. [ 2] Chemically, sirtuins are a class of proteins that possess either mono- ADP-ribosyltransferase or deacylase activity ...
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 ]
Sirtuin-activating compound. 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. [ 1]
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 ...
Sirtuin 3. 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.
51547 209011 Ensembl ENSG00000187531 ENSMUSG00000025138 UniProt Q9NRC8 Q8BKJ9 RefSeq (mRNA) NM_016538 NM_153056 NM_001363439 RefSeq (protein) NP_057622 NP_694696 NP_001350368 Location (UCSC) Chr 17: 81.91 – 81.92 Mb Chr 11: 120.51 – 120.52 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse NAD-dependent deacetylase sirtuin 7 is an enzyme that in humans is encoded by the SIRT7 gene ...
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