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Literature summary for 6.2.1.1 extracted from
- Evidence that ferredoxin interfaces with an internal redox shuttle in acetyl-CoA synthase during reductive activation and catalysis (2011), Biochemistry, 50, 276-286.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| reduced ferredoxin | required | Moorella thermoacetica |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of C-terminally His-tagged ACS in Escherichia coli strain BL21(DE3) | Moorella thermoacetica |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + acetate + CoA | Moorella thermoacetica | reaction of acetylated ACS with CoA and Fd-II, a step of the catalytic cycle in which the acetylated ACS reacts with CoA to form acetyl-CoA | AMP + diphosphate + acetyl-CoA | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Moorella thermoacetica | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant C-terminally His-tagged ACS from Escherichia coli strain BL21(DE3) by nickel affinity chromatography under anaerobic conditions | Moorella thermoacetica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + acetate + CoA | - |
Moorella thermoacetica | AMP + diphosphate + acetyl-CoA | - |
? | |
| ATP + acetate + CoA | reaction of acetylated ACS with CoA and Fd-II, a step of the catalytic cycle in which the acetylated ACS reacts with CoA to form acetyl-CoA | Moorella thermoacetica | AMP + diphosphate + acetyl-CoA | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Acetyl-CoA synthase | - |
Moorella thermoacetica |
| ACS | - |
Moorella thermoacetica |
| More | acetyl-CoA synthase is a subunit of the bifunctional CO dehydrogenase/acetyl-CoA synthase, CODH/ACS, complex | Moorella thermoacetica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 27 | - |
CO/acetyl-CoA exchange assay at | Moorella thermoacetica |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.2 | - |
CO/acetyl-CoA exchange assay at | Moorella thermoacetica |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Moorella thermoacetica |
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Release 2023.1 (January 2023)
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