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Literature summary 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

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.1.169 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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2.3.1.169 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

EC Number Organism UniProt Comment Textmining
2.3.1.169 Methanosarcina barkeri
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2.3.1.169 Moorella thermoacetica
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Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.169 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
2.3.1.169 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)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.169 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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2.3.1.169 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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2.3.1.169 CO2 + H+ + electron CO dehydrogenase catalyses the two-electron reduction of CO2 to CO Methanosarcina barkeri CO + H2O
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2.3.1.169 CO2 + H+ + electron CO dehydrogenase catalyses the two-electron reduction of CO2 to CO Moorella thermoacetica CO + H2O
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2.3.1.169 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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2.3.1.169 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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2.3.1.169 additional information the bifuctional enzyme CO dehydrogenase/acetyl-CoA synthase is central to the Wood-Ljungdahl pathway of autotrophic CO2 fixation Methanosarcina barkeri ?
-
?
2.3.1.169 additional information the bifuctional enzyme CO dehydrogenase/acetyl-CoA synthase is central to the Wood-Ljungdahl pathway of autotrophic CO2 fixation Moorella thermoacetica ?
-
?