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Literature summary for 2.3.1.169 extracted from

  • Lu, W.P.; Ragsdale, S.W.
    Reductive activation of the coenzyme A/acetyl-CoA isotopic exchange reaction catalyzed by carbon monoxide dehydrogenase from Clostridium thermoaceticum and its inhibition by nitrous oxide and carbon monoxide (1991), J. Biol. Chem., 266, 3554-3564.
    View publication on PubMed
Search for more literature for 2.3.1.169

Activating Compound

Activating Compound Comment Organism Structure
CO two effects: stimulation and inhibition on CoA/acetylCoA exchange Moorella thermoacetica

General Stability

General Stability Organism
reactions in presence of DTT, since enzyme requires strictly anaerobic conditions for stability Moorella thermoacetica

Inhibitors

Inhibitors Comment Organism Structure
CN- inhibitor on the CoA/acetyl-CoA exchange, 98% inhibition at 1.2 mM Moorella thermoacetica
CO non-competitive inhibitor on the CoA/acetyl-CoA exchange, the Ni-Fe-C-center appears to be the inhibitor site for CO Moorella thermoacetica
CO2 inhibitor on the CoA/acetyl-CoA exchange Moorella thermoacetica
dephospho-CoA inhibitor on the CoA/acetyl-CoA exchange, 75% inhibition at 0.44 mM Moorella thermoacetica
desulfo-CoA inhibitor on the CoA/acetyl-CoA exchange, 30% mM at 2.1 mM Moorella thermoacetica
N2O inhibitor on the CoA/acetyl-CoA exchange Moorella thermoacetica

Metals/Ions

Metals/Ions Comment Organism Structure
Fe corrinoid/iron-sulfur protein required Moorella thermoacetica
Fe the enzyme-bound complex can be described as an [NiFe3-4S4]-acetyl complex Moorella thermoacetica
Ni the enzyme-bound complex can be described as an [NiFe3-4S4]-acetyl complex Moorella thermoacetica

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
150000
-
-
 Moorella thermoacetica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Moorella thermoacetica key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway ?
-
 ?

Organism

Organism UniProt Comment Textmining
Moorella thermoacetica
-
-
-

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
a
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] Enzyme accepts the methyl group from the methylated corrinoid/iron-sulfur protein, binds a carbonyl group from CO, CO2, or the carboxyl of pyruvate, and binds coenzyme A. Then the enzyme catalyses the synthesis of acetyl-CoA from these enzyme bound groups. Additionally the enzyme catalyses two exchange reactions between the methylated corrinoid/iron-sulfur protein and methylated enzyme and between methylated enzyme and the methyl moiety of acetyl-CoA. Moorella thermoacetica
a
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] the enzyme-bound complex is an [NiFe3-4S4]-acetyl complex Moorella thermoacetica
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
28
-
 40°C, CoA/acetyl-CoA exchange Moorella thermoacetica

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
CH3-(corrinoid/iron-sulfur protein) + CO + HS-CoA under anaerobic conditions Moorella thermoacetica CH3-CO-S-CoA + corrinoid/iron-sulfur protein
-
 ?
CO + methyl-X + HS-CoA
-
 Moorella thermoacetica CH3-CO-S-CoA + HX
-
 ?
additional information enzyme catalyses the CoA/acetyl-CoA exchange Moorella thermoacetica ?
-
 ?
additional information key enzyme in the autotrophic acetyl-CoA pathway, i.e. Wood pathway, enzyme catalyses the final steps in this pathway Moorella thermoacetica ?
-
 ?

Subunits

Subunits Comment Organism
dimer alpha,beta Moorella thermoacetica

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Moorella thermoacetica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.7 7 optimum for CoA/acetyl-CoA exchange Moorella thermoacetica

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.4
-
 CO pH 7.0, 25°C, under anaerobic conditions, noncompetitive with respect to acetyl-CoA Moorella thermoacetica