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Literature summary for 2.3.1.169 extracted from

  • Seravalli, J.; Brown, K.L.; Ragsdale, S.W.
    Acetyl Coenzyme A synthesis from unnatural methylated corrinoids: Requirement for "Base-Off" coordination at cobalt (2001), J. Am. Chem. Soc., 123, 1786-1787.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
CO cobalt is the active site for the methyl–transfer reaction Methanosarcina barkeri
CO cobalt is the active site for the methyl–transfer reaction Moorella thermoacetica

Natural Substrates/ Products (Substrates)

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 ?
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additional information Moorella thermoacetica the bifuctional enzyme CO dehydrogenase/acetyl-CoA synthase is central to the Wood-Ljungdahl pathway of autotrophic CO2 fixation ?
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Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri
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Moorella thermoacetica
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Reaction

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 and Products (Substrate)

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
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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
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CO2 + H+ + electron CO dehydrogenase catalyses the two-electron reduction of CO2 to CO Methanosarcina barkeri CO + H2O
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CO2 + H+ + electron CO dehydrogenase catalyses the two-electron reduction of CO2 to CO Moorella thermoacetica CO + H2O
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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 ?
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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 ?
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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 ?
-
?