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Literature summary for 2.3.1.169 extracted from

  • Roberts, J.R.; Lu, W.P.; Ragsdale, S.W.
    Acetyl-coenzyme A synthesis from methyltetrahydrofolate, CO, and coenzyme A by enzymes purified from Clostridium thermoaceticum: Attainment of in vivo rates and identification of rate-limiting steps (1992), J. Bacteriol., 174, 4667-4676.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Ferredoxin stimulates the rate of synthesis of acetyl-CoA 4fold, Km is 0.0034 mM Moorella thermoacetica

General Stability

General Stability Organism
the acetyl-CoA synthesis is dependent on ionic strength, the CO/acetyl-CoA exchange is independent of ionic strength Moorella thermoacetica

Metals/Ions

Metals/Ions Comment Organism Structure
Fe corrinoid/iron-sulfur protein required Moorella thermoacetica

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Moorella thermoacetica enzyme and a corrinoid/iron-sulfur protein, methyltransferase and an electron transfer protein such as ferredoxin II play a pivotal role in the conversion of methylhydrofolate, CO, and CoA to acetyl-CoA ?
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Organism

Organism UniProt Comment Textmining
Moorella thermoacetica
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DSM 521
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Purification (Commentary)

Purification (Comment) Organism
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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
acetyl-CoA + a [Co(I) corrinoid Fe-S protein] = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein] enzyme contains binding sites for the methyl, carbonyl, and CoA moieties of acetyl-CoA and catalyses the assembly of acetyl-CoA from these enzyme-bound groups, under optimal conditions the rate-limiting step involves methylation of enzyme by the methylated corrinoid/iron-sulfur protein Moorella thermoacetica

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.12
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pH 6.8, acetyl-CoA synthesis, in absence of ferredoxin II Moorella thermoacetica
0.41
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pH 6.8, acetyl-CoA synthesis, in presence of 1 mM ferrous ammonium sulfate Moorella thermoacetica
0.49
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pH 6.8, acetyl-CoA synthesis, in presence of ferredoxin II Moorella thermoacetica
0.74
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pH 6.8, acetyl-CoA synthesis, in presence of 4 mM ATP Moorella thermoacetica
0.8
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pH 6.8, acetyl-CoA synthesis, in absence of ATP and Fe2+ 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
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CH3-tetrahydrofolate + CO + HS-CoA this multistep reaction involves four proteins: CO dehydrogenase, methyltransferase, the corrinoid/iron-sulfur protein and ferredoxin Moorella thermoacetica CH3-CO-S-CoA + tetrahydrofolate
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?
CH3I + CO + HS-CoA
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Moorella thermoacetica CH3-CO-S-CoA + HI
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CO + methyl-X + HS-CoA
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Moorella thermoacetica CH3-CO-S-CoA + HX
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?
additional information enzyme and a corrinoid/iron-sulfur protein, methyltransferase and an electron transfer protein such as ferredoxin II play a pivotal role in the conversion of methylhydrofolate, CO, and CoA to acetyl-CoA Moorella thermoacetica ?
-
?

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
25 35 in 10 mM Tris-maleate buffer and pH 5.8, the rate of acetyl-CoA synthesis is increased 2fold at 25°C to 35°C Moorella thermoacetica

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4
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CO/acetyl-CoA exchange reaction Moorella thermoacetica