EC Number   |
Natural Substrates |
|---|
   2.3.1.B43 | more |
it is proposed that YfiQ and CobB catalyze the reversible acetylation of a protein that mediates carbon-induced cpxP transcription |
| 2.3.1.B43 | more |
Sirt5 catalyzes the desuccinylation of histone peptides, molecular mechanism, overview. Human Sirt5 is a ubiquitous desuccinylase that catalyzes the desuccinylation of diverse histone succinyl sites with sequence selectivity. Among the 13 identified sites, H2BK116su is the most favorable Sirt5 substrate, with H4K12su showing the lowest catalytic efficiency and no activity observed in the presence of H4K31su |
| 2.3.1.B43 | more |
SIRT5 catalyzes the removal of negatively charged lysine acyl modifications: succinyl, malonyl, and glutaryl groups. SIRT5 is selective only for 3-5 carbon chains acidic acyl modifications, and displays no detectable activity against either an acetyl modification, a neutral 2 carbon group, or an adipoyl, a 6-carbon acidic modification |
| 2.3.1.B43 | more |
SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II. Mass spectrometry identifies 14 SIRT5 target sites on the SDHA subunit of Complex II and another eight on SDHB. Molecular modeling reveals that six of the eight SIRT5 target sites on SDHB orient toward the predicted membrane interface where SDHB interacts with SDHC/SDHD |
| 2.3.1.B43 | more |
SIRT5 modifies lysine succinylation, malonylation, and glutarylation |
| 2.3.1.B43 | more |
three-dimensional modeling of Complex II suggests that several SIRT5-targeted lysine residues lie at the protein-lipid interface of succinate dehydrogenase subunit B. Succinylation at these sites may disrupt Complex II subunit-subunit interactions and electron transfer. SIRT5 electrostatically binds to cardiolipin and desuccinylates mitochondrial inner membrane proteins including multiple subunits of all four electron transport chain (ETC) complexes and ATP synthase. SIRT5 targets lysines at the protein-lipid interface of Complex II |
| 2.3.1.B43 | NAD+ + [acetyl-coenzyme A synthetase]-N6-acetyl-L-lysine609 |
deacetylation by CobB activates the acetyl-coenzyme A synthetase |
| 2.3.1.B43 | NAD+ + [ATP synthase]-N6-succinyl-L-lysine |
- |
| 2.3.1.B43 | NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine |
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle. Deacetylation of CPS1 by SIRT5 results in activation of CPS1 enzymatic activity |
| 2.3.1.B43 | NAD+ + [carbamoyl phosphate synthase 1]-N6-acetyl-L-lysine |
SIRT5 deacetylates carbamoyl phosphate synthetase 1 (CPS1), an enzyme which is the first and rate-limiting step of urea cycle |
