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Literature summary extracted from

  • Seravalli, J.; Ragsdale, S.W.
    Pulse-chase studies of the synthesis of acetyl-CoA by carbon monoxide dehydrogenase/acetyl-CoA synthase: evidence for a random mechanism of methyl and carbonyl addition (2008), J. Biol. Chem., 283, 8384-8394.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.3.1.169 expression in Escherichia coli Moorella thermoacetica

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.2.7.4 72000
-
 beta subunit, SDS-PAGE Methanosarcina thermophila

Organism

EC Number Organism UniProt Comment Textmining
1.2.7.4 Methanosarcina thermophila
-
 strain DSM 521
-
1.2.7.4 Moorella thermoacetica
-
 strain DSM 521
-
2.3.1.169 Moorella thermoacetica P27988
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.2.7.4
-
 Moorella thermoacetica

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] CoA is the last substrate to bind and CO and the methyl group bind randomly as the first substrate in acetyl-CoA synthesis Moorella thermoacetica
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.7.4 CO + H2O + acceptor
-
 Moorella thermoacetica CO2 + reduced acceptor
-
 r
1.2.7.4 CO + H2O + acceptor
-
 Methanosarcina thermophila CO2 + reduced acceptor
-
 ?
2.3.1.169 additional information CoA is the last substrate to bind and CO and the methyl group bind randomly as the first substrate in acetyl-CoA synthesis. In pulse-chase experiments, up to 100% of the methyl groups and CoA and up to 60-70% of the CO employed in the pulse phase can be trapped in the product acetyl-CoA Moorella thermoacetica ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.2.7.4 CODH beta subunit of the bifunctional carbon monoxide dehydrogenase/acetyl-CoA synthase complex Methanosarcina thermophila
1.2.7.4 CODHACS bifunctional enzyme, CODHACS is a macromolecular machine that catalyzes the last step of the Wood-Ljungdahl pathway of anaerobic carbon dioxide fixation Moorella thermoacetica