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Literature summary extracted from

  • Seravalli, J.; Zhao, S.; Ragsdale, S.W.
    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.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.245 methylcob(III)-amide product inhibition Moorella thermoacetica
2.1.1.245 tetrahydrofolate product inhibition Moorella thermoacetica
2.1.1.258 tetrahydrofolate competitive inhibitor Moorella thermoacetica
2.1.1.258 [methyl-Co(III) corrinoid Fe-S protein] competitive inhibitor Moorella thermoacetica

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.245 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
2.1.1.245 0.002
-
 tetrahydrosarcinapterin pH 7.6, 25°C Moorella thermoacetica
2.1.1.245 0.012
-
 a [methyl-Co(III) corrinoid Fe-S protein] pH 7.6, 25°C Moorella thermoacetica
2.1.1.258 0.002
-
 5-methyltetrahydrofolate in 50 mM MES, pH 5.1, at 25°C Moorella thermoacetica
2.1.1.258 0.012
-
 [Co(I) corrinoid Fe-S protein] in 50 mM MES, pH 5.1, at 25°C Moorella thermoacetica

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.245 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

EC Number Organism UniProt Comment Textmining
2.1.1.245 Moorella thermoacetica
-
-
-
2.1.1.258 Moorella thermoacetica
-
 formerly Clostridium thermoaceticum
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.258
-
 Moorella thermoacetica

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.245 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.245 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
2.1.1.245 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
2.1.1.245 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 ?
-
 ?
2.1.1.258 [Co(I) corrinoid Fe-S protein] + 5-methyltetrahydrofolate
-
 Moorella thermoacetica [methyl-Co(III) corrinoid Fe-S protein] + tetrahydrofolate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.1.1.245 methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase
-
 Moorella thermoacetica
2.1.1.245 MeTr
-
 Moorella thermoacetica
2.1.1.258 methyltetrahydrofolate:corrinoid/iron-sulfur protein methyltransferase
-
 Moorella thermoacetica
2.1.1.258 MeTr
-
 Moorella thermoacetica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.245 25
-
 assay at Moorella thermoacetica

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1.1.245 14.7
-
 tetrahydrosarcinapterin pH 7.6, 25°C Moorella thermoacetica
2.1.1.245 14.7
-
 a [methyl-Co(III) corrinoid Fe-S protein] pH 7.6, 25°C Moorella thermoacetica
2.1.1.258 14.7
-
 5-methyltetrahydrofolate in 50 mM MES, pH 5.1, at 25°C Moorella thermoacetica
2.1.1.258 14.7
-
 [Co(I) corrinoid Fe-S protein] in 50 mM MES, pH 5.1, at 25°C Moorella thermoacetica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.245 7.6
-
 assay at Moorella thermoacetica

General Information

EC Number General Information Comment Organism
2.1.1.245 metabolism the enzyme reaction initiates the unusual biological organometallic reaction sequence that constitutes the Wood-Ljungdahl or reductive acetyl-CoA pathway Moorella thermoacetica
2.1.1.258 metabolism the enzyme performs a key step in the Wood-Ljungdahl pathway of acetyl-CoA synthesis Moorella thermoacetica