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Literature summary for 2.3.1.169 extracted from

  • Tan, X.; Sewell, C.; Yang, Q.; Lindahl, P.A.
    Reduction and methyl transfer kinetics of the a subunit from acetyl Coenzyme A synthase (2003), J. Am. Chem. Soc., 125, 318-319.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Fe the Ni-Fe4S4-5C cluster of enzyme catalyses the reversible reduction of CO2 to CO and is located in the beta-subunit. Moorella thermoacetica
Fe corrinoid/iron-sulfur protein required Moorella thermoacetica
Ni the Ni-Fe4S4-5C cluster of enzyme catalyses the reversible reduction of CO2 to CO and is located in the beta-subunit. Moorella thermoacetica
Ni enzyme contains nickel in the A-cluster of the enzyme Moorella thermoacetica

Organism

Organism UniProt Comment Textmining
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] pathway Moorella thermoacetica
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] the Ni-Fe4S4-5C cluster of enzyme catalyses the reversible reduction of CO2 to CO and is located in the beta-subunit. CO generated at this site migrates through the tunnel to the A-cluster, located in the alpha-subunit, where it reacts with CoA and a methyl group to generate acetyl-CoA. During catalysis, the two sites are mechanistically coupled. Moorella thermoacetica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CO + H2O the NiFe4S4-5C cluster catalyses the reversible oxidation of CO to CO2 Moorella thermoacetica CO2 + H+ + electron
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r

Subunits

Subunits Comment Organism
tetramer alpha,beta, containing two unique Ni-Fe-S active sites connected by a molecular tunnel Moorella thermoacetica