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Literature summary for 2.3.1.169 extracted from

  • Jablonski, P.E.; Lu, W.P.; Ragsdale, S.W.; Ferry, J.G.
    Characterization of the metal centers of the corrinoid/iron-sulfur component of the carbon monoxide dehydrogenase enzyme complex from Methanosarcina thermophila by EPR spectroscopy and spectroelectrochemistry (1993), J. Biol. Chem., 268, 325-329.
    View publication on PubMed
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Metals/Ions

Metals/Ions Comment Organism Structure
CO a cobalt-containing Co/Fe-S component of multienzyme complex serves as a methyl carrier in the pathway of methane synthesis from acetate Methanosarcina thermophila
Fe corrinoid/iron-sulfur protein required Methanosarcina thermophila
Fe the multienzyme complex contains at least two protein components: a CO-oxidizing Ni/Fe-S component and a cobalt-containing Co/Fe-S component Methanosarcina thermophila
Ni the multienzyme complex contains at least two protein components: a CO-oxidizing Ni/Fe-S component and a cobalt-containing Co/Fe-S component Methanosarcina thermophila

Organism

Organism UniProt Comment Textmining
Methanosarcina thermophila
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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 multienzyme complex contains at least two protein components: a CO-oxidizing Ni/Fe-S component and a Co/Fe-S component Methanosarcina thermophila
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CH3I + CO + HS-CoA the multienzyme complex catalyses the acetyl-CoA synthesis from CH3I, CO and CoA as well as to cleave acetyl-CoA into its methyl, carbonyl, and CoA components as the first step in the catabolism of acetyl-CoA to methane and CO2 Methanosarcina thermophila CH3-CO-S-CoA + HI
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