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Literature summary for 2.1.1.245 extracted from
- Mechanism of transfer of the methyl group from (6S)-methyltetrahydrofolate to the corrinoid/iron-sulfur protein catalyzed by the methyltransferase from Clostridium thermoaceticum: a key step in the Wood-Ljungdahl pathway of acetyl-CoA synthesis (1999), Biochemistry, 38, 5728-5735.
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| methylcob(III)-amide | product inhibition | Moorella thermoacetica |  |
| tetrahydrofolate | product inhibition | Moorella thermoacetica | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | single-turnover stopped-flow studies, steady-state and pre-steady-state kinetic studies at different pH values and by kinetic simulations, random Bi-Bi reaction mechanism, detailed overview | Moorella thermoacetica | |
| 0.002 | - |
tetrahydrosarcinapterin | pH 7.6, 25°C | Moorella thermoacetica | |
| 0.012 | - |
a [methyl-Co(III) corrinoid Fe-S protein] | pH 7.6, 25°C | Moorella thermoacetica |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrosarcinapterin | Moorella thermoacetica | a pH-dependent conformational change is required for methyl transfer in the forward and reverse directions, but this step is not rate-limiting | a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrosarcinapterin | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Moorella thermoacetica | - |
- |
- |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrosarcinapterin = a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrosarcinapterin | random Bi-Bi mechanism of transfer of the methyl group from (6S)-methyltetrahydrofolate to the corrinoid/iron-sulfur protein: CH3-H4folate binds to MeTr in the unprotonated form and then undergoes rapid protonation. This protonation enhances the electrophilicity of the methyl group, in agreement with a 10fold increase in the pKa at N5 of CH3-H4folate. Next, the Co(I)-CFeSP attacks the methyl group in a rate-limiting SN2 reaction to form methylcob(III)amide. Finally, the products randomly dissociate. A pH-dependent conformational change is required for methyl transfer in the forward and reverse directions, a rate-limiting ionization of MeTr, not of CH3-H4folate, is responsible for the pH dependence of the methyl transfer reaction | Moorella thermoacetica |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrosarcinapterin | a pH-dependent conformational change is required for methyl transfer in the forward and reverse directions, but this step is not rate-limiting | Moorella thermoacetica | a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrosarcinapterin | - |
r | |
| a [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrosarcinapterin | a pH-dependent conformational change is required for methyl transfer in the forward and reverse directions, but this step is not rate-limiting, the pH-dependent protein conformational change in the ternary complex is linked to deprotonation of the active complexes | Moorella thermoacetica | a [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrosarcinapterin | - |
r | |
| additional information | the methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase catalyzes transfer of the N5-methyl group from (6S)-methyltetrahydrofolate, i.e. CH3-H4folate, to the cobalt center of a corrinoid/iron-sulfur protein, CFeSP, forming methylcob(III)-amide and H4folate | Moorella thermoacetica | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase | - |
Moorella thermoacetica |
| MeTr | - |
Moorella thermoacetica |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Moorella thermoacetica |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 14.7 | - |
tetrahydrosarcinapterin | pH 7.6, 25°C | Moorella thermoacetica | |
| 14.7 | - |
a [methyl-Co(III) corrinoid Fe-S protein] | pH 7.6, 25°C | Moorella thermoacetica |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.6 | - |
assay at | Moorella thermoacetica |
General Information
| General Information | Comment | Organism |
|---|---|---|
| metabolism | the enzyme reaction initiates the unusual biological organometallic reaction sequence that constitutes the Wood-Ljungdahl or reductive acetyl-CoA pathway | Moorella thermoacetica |
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