Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | reductive activation of the enzyme by ferrdoxin, mechanism, detailed overview | Moorella thermoacetica |
Cloned (Comment) | Organism |
---|---|
expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) from a pet29a(+) vector | Moorella thermoacetica |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Cu2+ | - |
Moorella thermoacetica | |
Fe2+ | in cofactor ferredoxin(II), which harbors two [4Fe-4S] clusters | Moorella thermoacetica | |
Zn2+ | - |
Moorella thermoacetica |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ni2+ | formation of the NiFeC species | Moorella thermoacetica |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + corrinoid protein | Moorella thermoacetica | - |
CoA + CO + methylcorrinoid protein | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Moorella thermoacetica | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant C-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography under a N2 atmosphere | Moorella thermoacetica |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] | the methyl and carbonyl groups bind to ACS in a random manner before the strictly ordered binding of the third substrate, CoA, mechanism of acetyl-CoA synthesis by ACS, overview | Moorella thermoacetica |
Renatured (Comment) | Organism |
---|---|
purified recombinant ACS is Ni-reconstituted in the elution buffer with 6 equivalents of NiCl2 for 2 or 3 days at 27°C or at 45°C | Moorella thermoacetica |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
acetyl-CoA + corrinoid protein | - |
Moorella thermoacetica | CoA + CO + methylcorrinoid protein | - |
? | |
acetyl-CoA + corrinoid protein | Fd-II can act as a redox mediator by accepting electrons from the acetyl-ACS intermediate and by serving as the initial reducing agent linked to formation of the Ni1+-CO catalytic intermediate | Moorella thermoacetica | CoA + CO + methylcorrinoid protein | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterotetramer | CODH and ACS make up the two subunits of a 310 kDa alpha2beta2 heterotetrameric enzymatic complex | Moorella thermoacetica |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
22 | - |
acetyl-CoA exchange assay at room temperature | Moorella thermoacetica |
45 | - |
methylation reaction assay at | Moorella thermoacetica |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.2 | - |
acetyl-CoA exchange assay at | Moorella thermoacetica |
7.6 | - |
methylation reaction assay at | Moorella thermoacetica |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
acetyl-CoA | - |
Moorella thermoacetica | |
Ferredoxin | Fd-II, which harbors two [4Fe-4S] clusters and is an electron acceptor for CODH, serves as a redox activator of ACS. Catalytic one-electron redox-active species in the CO/acetyl-CoA exchange reaction. Incubation of ACS with Fd-II and CO leads to the formation of the NiFeC species. FdII is purified from Moorella thermoacetica, overview | Moorella thermoacetica |
General Information | Comment | Organism |
---|---|---|
physiological function | acetyl-CoA synthase, ACS, 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 | Moorella thermoacetica |