EC Number   |
General Information |
Reference |
|---|
   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 |
| 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 |
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 | physiological function |
heterochromatin assembly requires the SIR proteins Sir3, the primary structural component of SIR heterochromatin, and the Sir2-4 complex, responsible for the targeted recruitment of SIR proteins and the deacetylation of lysine 16 of histone H4 |
752056 |
| 2.3.1.286 | physiological function |
increase of enzyme activity by caloric restriction or osmotic stress increases genome stability and lifespan in Saccharomyces cerevisiae |
750369 |
| 2.3.1.286 | physiological function |
increased enzyme expression of extends life span in a dose-dependent manner |
749528 |
| 2.3.1.286 | metabolism |
isoform SIRT3 levels modulate mitochondrial protein folding |
738661 |
| 2.3.1.286 | physiological function |
maintenance of [histone H3]-L-lysine9 methylation at centromeres requires the histone deacetylases Sir2 and Clr3 |
750413 |
| 2.3.1.286 | malfunction |
NAD+-dependent SIRT1 deactivation has a key role on ischemia-reperfusion-induced apoptosis |
739745 |
