The enzyme, which catalyses the transfer of a methyl group from tetramethylammonium to a tetramethylammonium-specific corrinoid protein (MtqC), is involved in methanogenesis from tetramethylammonium. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.253, methylated tetramethylammonium-specific corrinoid protein:coenzyme M methyltransferase.
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The expected taxonomic range for this enzyme is: Methanosarcina barkeri
The enzyme, which catalyses the transfer of a methyl group from tetramethylammonium to a tetramethylammonium-specific corrinoid protein (MtqC), is involved in methanogenesis from tetramethylammonium. Methylation of the corrinoid protein requires the central cobalt to be in the Co(I) state. During methylation the cobalt is oxidized to the Co(III) state. The methylated corrinoid protein is substrate for EC 2.1.1.253, methylated tetramethylammonium-specific corrinoid protein:coenzyme M methyltransferase.
cell extracts of strain NaT1 catalyze the formation of methyl-coenzyme M from coenzyme M and tetramethylammonium, EC 2.1.1.253, or trimethylamine, EC 2.1.1.250, but not from coenzyme M and dimethylamine, EC 2.1.1.249, monomethylamine, EC 2.1.1.248, or methanol, EC 2.1.1.246
cell extracts of strain NaT1 catalyze the formation of methyl-coenzyme M from coenzyme M and tetramethylammonium, EC 2.1.1.253, or trimethylamine, EC 2.1.1.250, but not from coenzyme M and dimethylamine, EC 2.1.1.249, monomethylamine, EC 2.1.1.248, or methanol, EC 2.1.1.246
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme by ultracentrifugation, a first step of anion exchange chromatography, hydroxyapatite chromatography, a second step of anion exchange chromatography, adsorption and again a third step of anion exchange chromatography
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2.1.1.252 tetramethylammonium-corrinoid protein Co-methyltransferase
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