Acetyl-CoA synthetase

Acetyl-CoA synthetase family contains two isoforms with different responsiveness to SIRT proteins: purified truncated recombinant mouse mitochondrial AceCS2 is fully inactivated upon acetylation and reactivated by SIRT3 at a rate about 5 times that of SIRT1; AceCS1 is efficiently deacetylated and activated by both SIRT1 and SIRT3 with an identical specificity constant of 3.2×10⁴ M^-1·s^-1, whereas SIRT2, SIRT5 and SIRT6 barely catalyze its deacetylation or have no activity at all^[1].
Acetyl-CoA synthetase displays species-specific catalytic differences: in 3 mM Ti³⁺ citrate without reducing agents, ACSCh and CODH/ACS_Ch from C. hydrogenoformans exhibit markedly higher CO-acetyl-CoA isotopic exchange and synthetic activity than CODH/ACS_Mt from M. thermoacetica^[2].
Acetyl-CoA synthetase randomly binds the methyl group derived from CFeSP and CO, and binds coenzyme A in an ordered manner; this enzyme is activated via reduction to generate an active Ni (I) state, which combines with CO to form an EPR-positive NiFeC intermediate. In CODH/ACS_Mt, the hydrophobic channel connecting the CODH C cluster and the ACS A cluster is responsible for the efficient transport of CO to enable CO₂-dependent acetyl-CoA synthesis, and is also involved in the synergistic inhibition of acetyl-CoA synthetase by exogenous CO^[2].
Acetyl-CoA synthetase 1 relies on SIRT1 for its acetylation modification and lipid metabolism regulation in Cos-7 cells^[1].

MedChemExpress (MCE) has not independently confirmed the accuracy of these methods. They are for reference only.