EC Number   |
General Information |
Reference |
|---|
    6.2.1.1 | metabolism |
acetyl-CoA synthase, a subunit of the bifunctional CO dehydrogenase/acetyl-CoA synthase, CODH/ACS, complex of Moorella thermoacetica requires reductive activation in order to catalyze acetyl-CoA synthesis and related partial reactions, including the CO/acetyl-CoA exchange reaction. Ferredoxin(II), which harbors two [4Fe-4S] clusters and is an electron acceptor for CODH, serves as a redox activator of ACS. Ferredoxin interfaces with an internal redox shuttle in acetyl-CoA synthase during reductive activation and catalysis. The midpoint reduction potential for the catalytic one-electron redoxactive species in the CO/acetyl-CoAexchange reaction is -511 mV. Incubation of ACS with Fd-II and CO leads to the formation of the NiFeC species. Mechanism, overview |
714240 |
| 6.2.1.1 | physiological function |
acetyl-CoA synthetase 2 is a regulator of autophagy and lifespan |
744651 |
| 6.2.1.1 | physiological function |
acetyl-coenzyme A synthetase activates acetate into acetyl-coenzyme A in most cells. Salmonella enterica requires Acs activity for growth on acetate. The sirtuin-dependent protein acylation/deacylation system, SDPADS, controls the activity of Acs |
716267 |
| 6.2.1.1 | physiological function |
activation of acetate in energy metabolism |
-, 726837 |
| 6.2.1.1 | metabolism |
activation of weak organic acids by acyl-CoA synthetases is costly to cells, since it requires 2 mol of ATP per mol of substrate; 1 mol of ATP is consumed to activate the organic acid, while the second mol of ATP is needed to convert AMP to ADP, the immediate precursor of ATP. Further loss of energy resources during the course of the Acs reaction is caused by the hydrolysis of diphosphate to monophosphate through pyrophosphate phosphohydrolase, EC 3.6.1.1 |
716267 |
| 6.2.1.1 | physiological function |
an acs2 deletion strain has a reduced replicative life span compared to wild-type and isoform acs1 deletion strains. Replicatively aged acs2 deletion cells contain elevated levels of extrachromosomal rDNA circles, and silencing at the rDNA locus is impaired in an acs2 deletion strain |
705678 |
| 6.2.1.1 | malfunction |
cyclic AMP inhibits the activity and promotes the acetylation of acetyl-CoA synthetase through competitive binding to the ATP/AMP pocket. cAMP directly binds to the enzyme and inhibits its activity in a substrate-competitive manner. cAMP binding increases SeAcs acetylation by simultaneously promoting Pat-dependent acetylation and inhibiting CobB-dependent deacetylation, resulting in enhanced SeAcs inhibition |
-, 745369 |
| 6.2.1.1 | malfunction |
decreased isoform ACSS2 expression inhibits renal cell carcinoma cell migration and invasion |
744665 |
| 6.2.1.1 | malfunction |
deletion of individual and multiple subunits of acetyl-CoA synthetase decreases CoA release activity for several different CoA ester substrates. Deletion of acetyl-CoA synthetases I and II increases production of 3-hydroxypropionate by the metabolically-engineered hyperthermophile Pyrococcus furiosus (containing three enzymes from the CO2 fixation cycle of the thermoacidophilic archaeon Metallosphaerasedula) |
725872 |
| 6.2.1.1 | physiological function |
enzyme overexpression results in higher resistance to acetic acid as measured by an increased growth rate and shorter lag phase relative to a wild type strain, suggesting that enzyme-mediated consumption of acetic acid during fermentation contributes to acetic acid detoxification |
744932 |
