2.1.1.246: [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase
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For detailed information about [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase, go to the full flat file.
Word Map on EC 2.1.1.246
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2.1.1.246
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methyltransferases
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euchromatic
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methanosarcina
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barkeri
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rna-directed
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methanogenesis
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monomethylamine
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24-nucleotide
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dimethylamine
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biofuel production
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synthesis
- 2.1.1.246
- methyltransferases
-
euchromatic
- methanosarcina
- barkeri
-
rna-directed
-
methanogenesis
- monomethylamine
-
24-nucleotide
- dimethylamine
- biofuel production
- synthesis
Reaction
Synonyms
Co-methyl-5-hydroxybenzimidazolylcobamide:2-mercapto-ethanesulphonic acid methyltransferase, methanol-specific methyltransferase 2, methanol:cob(I)alamin methyltransferase, methanol:coenzyme M methyltransferase, methylcobalamin:coenzyme M methyltransferase, methylcobamide:coenzyme M methyltransferase, methylcobamide:CoM methyltransferase, methyltransferase 2, MT2, MT2-A, MT2-M, mtaA
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General Information
General Information on EC 2.1.1.246 - [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase
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evolution
metabolism
physiological function
additional information
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Methanosarcina barkeri contains an isoenzyme of MtaA designated MtbA. The isoenzyme reacts with MtaC with only 2.5% of the activity of MtaA
evolution
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specific MT1/corrinoid pairs have been identified for methanol (MtaC, MtaB), trimethylamine (MttC, MttB), dimethylamine (MtbC, MtbB), methylamine (MtmC, MtmB) and methylsulfide (MtsA, MtsB). MT2 proteins are somewhat less specific with MtaA being used for methanol, and poorly for trimethylamine showing 5% of the methanol-dependent activity, and an enzyme designated MtbA, EC 2.1.1.1247, being used for all three methylamines. The MtsA protein apparently catalyses both MT1 and MT2 reactions in the activation of dimethylsulfide
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all combinations of MtaC, MtaB, and MtaA can form functional methanol-specific methyltransferase 1/2, MT1/MT2, complexes. Substrate-dependent, posttranscriptional regulation of mtaCBA operons, overview
metabolism
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methanol catabolism in Methanosarcina species requires the concerted effort of methanol:5-hydroxybenzimidazolylcobamide methyltransferase, MtaB, a corrinoid-containing methyl-accepting protein, MtaC, and Co-methyl-5-hydroxybenzimidazolylcobamide:2-mercapto-ethanesulfonic acid methyltransferase, MtaA
metabolism
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methyl-coenzyme M formation from coenzyme M and methanol in Methanosarcina barkeri is catalysed by an enzyme system composed of three polypeptides MtaA, MtaB and MtaC, the latter of which harbours a corrinoid prosthetic group. We report here that MtaC can be substituted by free cob(I)alamin which is methylated with methanol in an MtaB-catalysed reaction and demethylated with coenzyme M in an MtaA-catalysed reaction
metabolism
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the enzyme system catalyzing the formation of methyl-coenzyme M from methanol and coenzyme M in Methanosarcina barkeri is composed of the three different polypeptides MtaA, MtaB and MtaC of which MtaC harbors a corrinoid prosthetic group
metabolism
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the enzyme system from Methanosarcina barkeri is composed of two methyltransferases, transferase MT1, which is composed of a 50-kDa subunit, MtaB, and a 27-kDa corrinoid-harbouring subunit, MtaC, catalyzes the methylation of free cob(1)alamin with methanol, EC 2.1.1.90, and transferase MT2 catalyzes the transfer of the methyl group from CH,-MT1 to coenzyme M. Instead of CH,-MTI, MtaA can also use free methylcobalamin as the methyl donor. MtaC with its supernucleophilic cobamide prosthetic group accepts the methyl group from methanol and passes it to coenzyme M, MtaB activates methanol for nucleophilic attack by the cob(1)amide, and MtaA activates coenzyme M for nucleophilic attack of the methyl group of the methylcobamide
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a positive effect of MtaA on the catalytic efficiency of MtaB is specific for MtaA. In the absence of MtaA no effect is observed, while in the presence of MtaA the formation of methylcob(III)alamin from methanol and cob(I)alamin is apparently inhibited by coenzyme M, probably because under these conditions MtaA actively catalyses the demethylation of methylcob(III)alamin. MtaB plus methanol positively affect the catalytic efficiency of MtaA
physiological function
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the methyltransferase designated MtaA together with the proteins MtaB and MtaC mediate the formation of methyl-coenzyme M from methanol and coenzyme M. MtaC is a 28-kDa corrinoid protein, MtaB, EC 2.1.1.90, catalyzes the methylation of MtaC and MtaA catalyzes the demethylation of methylated MtaC
physiological function
methanol:coenzyme M methyltransferase is an enzyme complex composed of three subunits, MtaA, MtaB, and MtaC, found in methanogenic archaea and is needed for their growth on methanol ultimately producing methane. MtaABC catalyzes the energetically favorable methyl transfer from methanol to coenzyme M to form methyl coenzyme M, an important reaction for possible production of methanol from the anaerobic oxidation of methane
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MtaC and MtaB form a tight complex and the encoding genes form a transcription unit, whereas MtaA purifies separately and its encoding gene is located separately
additional information
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the enzyme system catalyzing the formation of methyl-coenzyme M from methanol and coenzyme M in Methanosarcina barkeri is composed of the three different polypeptides MtaA, MtaB and MtaC of which MtaC harbors a corrinoid prosthetic group
additional information
enzyme complex structure analysis and structure-function analysis, overview