2.1.1.246: [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase
This is an abbreviated version!
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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Metals Ions
Metals Ions on EC 2.1.1.246 - [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M methyltransferase
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Co2+
Zn2+
additional information
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Zn21 or Co21 are required for MtaA activity, Zn2+ can be replaced by Co2+ but not by Mg2+, the kinetics of activation by Co2+ being similarily slow. About 1 mol of transition metal is bound per mol of protein. The role of the transition metal in MtaA is to lower the microscopic pKa of the thiol group of coenzyme M by coordination to the zinc, and thus to increase its nucleophilicity for methyl group attack, pKZn2+ of MtaA is over 15
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required, the apoprotein reacts with zinc or cobalt to the fully active holoenzyme
Zn2+
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1 mol per mol of enzyme, required, the apoprotein reacts with zinc or cobalt to the fully active holoenzyme
Zn2+
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dependent on, wild-type MtaA has a zinc content of 0.91 mol/mol, binding structure, overview
Zn2+
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Mta contains 1 mol Zn2+ per mol of enzyme, Zn2+ can be substituted by Co2+