Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
CO | cobalt is the active site for the methyltransfer reaction | Methanosarcina barkeri | |
CO | cobalt is the active site for the methyltransfer reaction | Moorella thermoacetica |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Methanosarcina barkeri | the bifuctional enzyme CO dehydrogenase/acetyl-CoA synthase is central to the Wood-Ljungdahl pathway of autotrophic CO2 fixation | ? | - |
? | |
additional information | Moorella thermoacetica | the bifuctional enzyme CO dehydrogenase/acetyl-CoA synthase is central to the Wood-Ljungdahl pathway of autotrophic CO2 fixation | ? | - |
? |
Organism | UniProt | Comment | Textmining |
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Methanosarcina barkeri | - |
- |
- |
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 transfer of Co bound methyl group from methylated corrinoid/iron-sulfur protein to acetyl-CoA synthase is an SN2 attack of a nucleophilic center of enzyme, presumably Ni4, on the methyl-Co(III) stat of the corrinoid/iron-sulfur protein, generating Co(I) and methylating acetyl-CoA synthase. | Methanosarcina barkeri | |
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] | The transfer of Co bound methyl group from methylated corrinoid/iron-sulfur protein to acetyl-CoA synthase is an SN2 attack of a nucleophilic center of enzyme, presumably Ni4, on the methyl-Co(III) stat of the corrinoid/iron-sulfur protein, generating Co(I) and methylating acetyl-CoA synthase. | Moorella thermoacetica |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
CO + methyl-X + HS-CoA | acetyl-CoA synthase catalyses acetyl-CoA synthesis, an intermediate step is the transfer of the cobalt-bound methyl group from methylated corrinoid/iron-sulfur protein to the acetyl-CoA synthase | Methanosarcina barkeri | CH3-CO-S-CoA + HX | - |
? | |
CO + methyl-X + HS-CoA | acetyl-CoA synthase catalyses acetyl-CoA synthesis, an intermediate step is the transfer of the cobalt-bound methyl group from methylated corrinoid/iron-sulfur protein to the acetyl-CoA synthase | Moorella thermoacetica | CH3-CO-S-CoA + HX | - |
? | |
CO2 + H+ + electron | CO dehydrogenase catalyses the two-electron reduction of CO2 to CO | Methanosarcina barkeri | CO + H2O | - |
? | |
CO2 + H+ + electron | CO dehydrogenase catalyses the two-electron reduction of CO2 to CO | Moorella thermoacetica | CO + H2O | - |
? | |
additional information | methylcobinamide, methylcobalamin, and CH3-(Me3-benzimidazolyl)cobamide are substrates of the acetyl-CoA synthase, methylcobalamin is 2000fold less reactive than methylcobinamide, CO dehydrogenase catalyses the CO-dependent reduction of methylcobinamide 10000fold faster than that of methylcobalamin | Methanosarcina barkeri | ? | - |
? | |
additional information | methylcobinamide, methylcobalamin, and CH3-(Me3-benzimidazolyl)cobamide are substrates of the acetyl-CoA synthase, methylcobalamin is 2000fold less reactive than methylcobinamide, CO dehydrogenase catalyses the CO-dependent reduction of methylcobinamide 10000fold faster than that of methylcobalamin | Moorella thermoacetica | ? | - |
? | |
additional information | the bifuctional enzyme CO dehydrogenase/acetyl-CoA synthase is central to the Wood-Ljungdahl pathway of autotrophic CO2 fixation | Methanosarcina barkeri | ? | - |
? | |
additional information | the bifuctional enzyme CO dehydrogenase/acetyl-CoA synthase is central to the Wood-Ljungdahl pathway of autotrophic CO2 fixation | Moorella thermoacetica | ? | - |
? |