EC Number |
General Information |
Reference |
---|
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 |