2.3.1.286	metabolism	Sir2 is involved in the regulation of p53 function via deacetylation	729560	
2.3.1.286	metabolism	SIRT1 modulates DNA repair activity, which can be regulated by the acetylation status of repair protein Ku70 following DNA damage	729683	
2.3.1.286	metabolism	the deacetylation of [histone H4]-N6-acetyl-L-lysine16 by Sirt2 may be pivotal to the formation of condensed chromatin	729802	
2.3.1.286	metabolism	acetylation of Lys413 decreases catalysis and SIRT3 reactivates isocitrate dehydrogenase 2 upon deacetylation. SIRT3-dependent deacetylation of isocitrate dehydrogenase 2 suppresses cellular stress by reactive oxygen species (ROS). Acetylation of Lys413 is regulated by SIRT3 in response to calorie and glucose restriction	729982	
2.3.1.286	metabolism	the enzyme can regulate flux and anapleurosis of this central metabolic cycle	730205	
2.3.1.286	metabolism	caloric restriction can extend life-span by inducing SIRT1 expression and promoting the long-term survival of irreplaceable cells	730962	
2.3.1.286	physiological function	enzyme expression is crucial for the survival of the cell	737969	
2.3.1.286	malfunction	SIRT1 depletion by RNA interference attenuates capsaicin-induced apoptosis in A-549 cancer cells and autophagy in MRC-5 cells	738438	
2.3.1.286	metabolism	isoform SIRT3 levels modulate mitochondrial protein folding	738661	
2.3.1.286	physiological function	acetylation of heat shock protein 10 by isoform SIRT3 enhances medium-chain acyl-CoA dehydrogenase folding, enzyme activity, and fat oxidation	738661