2.1.1.251: methylated-thiol-coenzyme M methyltransferase
This is an abbreviated version!
For detailed information about methylated-thiol-coenzyme M methyltransferase, go to the full flat file.
Reaction
Synonyms
480-kDa CoM methylase, CoM methylase, DMS:CoM methyltransferase, methylthiol:coenzyme M methyltransferase, methylthiol:CoM methyltransferase, methyltransferase II, MMPA:CoM methyltransferase, MtsA
ECTree
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General Information
General Information on EC 2.1.1.251 - methylated-thiol-coenzyme M methyltransferase
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evolution
the sequence of MtsA is homologous to the A and M isozymes of methylcobamide:coenzyme M methyltransferases (methyltransferase II), indicating that the alpha polypeptide is a member of the methyltransferase II family of coenzyme M methylases
metabolism
physiological function
additional information
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pathways of dimethylsulfide- and methanethiol-dependent CoM methylation are regulated. Stimulation of methanogenesis in cell extract is due to the inherent ability of the purified 480-kDa CoM methylase to function as a methylthiol:CoM methyltransferase. In the case of CoM methylation by trimethylamine, dimethylamine, monomethylamine, or methanol, separate proteins specific for each substrate exist
metabolism
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pathways of dimethylsulfide- and methanethiol-dependent CoM methylation are regulated. Stimulation of methanogenesis in cell extract is due to the inherent ability of the purified 480-kDa CoM methylase to function as a methylthiol:CoM methyltransferase. In the case of CoM methylation by trimethylamine, dimethylamine, monomethylamine, or methanol, separate proteins specific for each substrate exist
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metabolism
Methanosarcina barkeri Fusaro / DSM 804
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pathways of dimethylsulfide- and methanethiol-dependent CoM methylation are regulated. Stimulation of methanogenesis in cell extract is due to the inherent ability of the purified 480-kDa CoM methylase to function as a methylthiol:CoM methyltransferase. In the case of CoM methylation by trimethylamine, dimethylamine, monomethylamine, or methanol, separate proteins specific for each substrate exist
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methanogenesis from dimethylsulfide requires the intermediate methylation of coenzyme M. This reaction is catalyzed by a methylthiol:coenzymeMmethyltransferase composed of two polypeptides, MtsA, which is a methylcobalamin:coenzyme M methyltransferase, and MtsB, which is homologous to a class of corrinoid proteins involved in methanogenesis. MtsA is an active methylcobalamin:coenzyme M methyltransferase, but also methylates cob(I)alamin with dimethylsulfide, yielding equimolar methylcobalamin and methanethiol
physiological function
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the 480-kDa corrinoid protein functions as a CoM methylase during methanogenesis from dimethylsulfide and methylmercaptopropionate, since the monomethylamine corrinoid protein and the A isozyme of methylcobamide:CoM methyltransferase, EC 2.1.1.247, do not catalyze CoM methylation with methylated thiols
physiological function
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the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate
physiological function
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the 480-kDa corrinoid protein functions as a CoM methylase during methanogenesis from dimethylsulfide and methylmercaptopropionate, since the monomethylamine corrinoid protein and the A isozyme of methylcobamide:CoM methyltransferase, EC 2.1.1.247, do not catalyze CoM methylation with methylated thiols
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physiological function
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the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate
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physiological function
Methanosarcina barkeri Fusaro / DSM 804
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the 480-kDa corrinoid protein functions as a CoM methylase during methanogenesis from dimethylsulfide and methylmercaptopropionate, since the monomethylamine corrinoid protein and the A isozyme of methylcobamide:CoM methyltransferase, EC 2.1.1.247, do not catalyze CoM methylation with methylated thiols
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methylated thiol-dependent methanogenesis in cell extract is a function of the growth substrate, methanogenesis from either diethylsulfide or methylmercaptopropionate in cell extracts is coupled with the formation of methanethiol or mercaptopropionate, respectively. Consumption of methanethiol itself for methane formation also occurs. Dimethylsulfide is converted to methane by an initial demethylation which results in the formation of methanethiol. number of other compounds, including dimethylsulfoniopropionate, alanine, methionine, glycine, sarcoscine, N,N-dimethyl glycine, betaine, trimethylamine, choline, creatinine, and acetone, are not converted to methane at significant rates
additional information
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methylated thiol-dependent methanogenesis in cell extract is a function of the growth substrate, methanogenesis from either diethylsulfide or methylmercaptopropionate in cell extracts is coupled with the formation of methanethiol or mercaptopropionate, respectively. Consumption of methanethiol itself for methane formation also occurs. Dimethylsulfide is converted to methane by an initial demethylation which results in the formation of methanethiol. number of other compounds, including dimethylsulfoniopropionate, alanine, methionine, glycine, sarcoscine, N,N-dimethyl glycine, betaine, trimethylamine, choline, creatinine, and acetone, are not converted to methane at significant rates
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additional information
Methanosarcina barkeri Fusaro / DSM 804
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methylated thiol-dependent methanogenesis in cell extract is a function of the growth substrate, methanogenesis from either diethylsulfide or methylmercaptopropionate in cell extracts is coupled with the formation of methanethiol or mercaptopropionate, respectively. Consumption of methanethiol itself for methane formation also occurs. Dimethylsulfide is converted to methane by an initial demethylation which results in the formation of methanethiol. number of other compounds, including dimethylsulfoniopropionate, alanine, methionine, glycine, sarcoscine, N,N-dimethyl glycine, betaine, trimethylamine, choline, creatinine, and acetone, are not converted to methane at significant rates
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