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Literature summary for 2.3.1.169 extracted from

  • Grahame, D.A.
    Substrate and cofactor reactivity of a carbon monoxide dehydrogenase-corrinoid enzyme complex: stepwise reduction of iron-sulfur and corrinoid centers, the corrinoid Co2+/1+ redox midpoint potential, and overall synthesis of acetyl-CoA (1993), Biochemistry, 32, 10786-10793.
    View publication on PubMed
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Metals/Ions

Metals/Ions Comment Organism Structure
Fe corrinoid/iron-sulfur protein required Methanosarcina barkeri

Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri
-
-
-

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] pathway Methanosarcina barkeri
a
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] the corronoid protein functions as methyl group carrier during acetyl-CoA synthesis and decomposition Methanosarcina barkeri
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CH3-CO-S-CoA + tetrahydrosarcinapterin + H2O the carbon monoxide dehydrogenase-corrinoid enzyme complex catalyzes the cleavage of acetyl-CoA, tetrahydrosarcinapterin functions as the methyl group acceptor, the major products of reaction are methyltetrahydrosarcinapterin and CO2, free CoA is identified as an additional product Methanosarcina barkeri CH3-tetrahydrosarcinapterin + CO2 + H+ + electron
-
 ?
CH3-tetrahydrosarcinapterin + CO + HS-CoA
-
 Methanosarcina barkeri CH3-CO-S-CoA + tetrahydrosarcinapterin
-
 ?
CO + H2O
-
 Methanosarcina barkeri CO2 + H+ + electron
-
 r
CO + methyl-X + HS-CoA
-
 Methanosarcina barkeri CH3-CO-S-CoA + HX
-
 ?