Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Ferredoxin | stimulates the rate of synthesis of acetyl-CoA 4fold, Km is 0.0034 mM | Moorella thermoacetica |
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 | Comment | Organism | Structure |
---|---|---|---|
Fe | corrinoid/iron-sulfur protein required | Moorella thermoacetica |
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 | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Moorella thermoacetica | - |
DSM 521 | - |
Purification (Comment) | Organism |
---|---|
- |
Moorella thermoacetica |
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 Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.12 | - |
pH 6.8, acetyl-CoA synthesis, in absence of ferredoxin II | Moorella thermoacetica |
0.41 | - |
pH 6.8, acetyl-CoA synthesis, in presence of 1 mM ferrous ammonium sulfate | Moorella thermoacetica |
0.49 | - |
pH 6.8, acetyl-CoA synthesis, in presence of ferredoxin II | Moorella thermoacetica |
0.74 | - |
pH 6.8, acetyl-CoA synthesis, in presence of 4 mM ATP | Moorella thermoacetica |
0.8 | - |
pH 6.8, acetyl-CoA synthesis, in absence of ATP and Fe2+ | Moorella thermoacetica |
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 | - |
? | |
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 | - |
? | |
CH3I + CO + HS-CoA | - |
Moorella thermoacetica | CH3-CO-S-CoA + HI | - |
? | |
CO + methyl-X + HS-CoA | - |
Moorella thermoacetica | CH3-CO-S-CoA + HX | - |
? | |
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 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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.4 | - |
CO/acetyl-CoA exchange reaction | Moorella thermoacetica |