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Literature summary extracted from

  • Krüer, M.; Haumann, M.; Meyer-Klaucke, W.; Thauer, R.; Dau, H.
    The role of zinc in the methylation of the coenzyme M thiol group in methanol:coenzyme M methyltransferase from Methanosarcina barkeri: new insights from X-ray absorption spectroscopy (2002), Eur. J. Biochem., 269, 2117-2123.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.1.1.251 additional information ATP and/or MgCl2 do not stimulate the MMPA:CoM methyltransferase reactions mediated by the purified methylthiol: CoM methyltransferase Methanosarcina barkeri
2.1.1.251 Ti(III) citrate not essential activation Methanosarcina barkeri

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.246 gene mtaA, sequence comparison, expression of His-tagged MtaA in Escherichia coli strain M15 Methanosarcina barkeri

Protein Variants

EC Number Protein Variants Comment Organism
2.1.1.246 C239A site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme Methanosarcina barkeri
2.1.1.246 H237A site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme Methanosarcina barkeri

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.246 Zn2+ dependent on, wild-type MtaA has a zinc content of 0.91 mol/mol, binding structure, overview Methanosarcina barkeri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.251 480000
-
-
 Methanosarcina barkeri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.246 a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M Methanosarcina barkeri
-
 methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
 r
2.1.1.246 a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M Methanosarcina barkeri Fusaro, DSM 804
-
 methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
 r
2.1.1.246 a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M Methanosarcina barkeri Fusaro / DSM 804
-
 methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
 r
2.1.1.251 dimethylsulfide + coenzyme M Methanosarcina barkeri
-
 methyl-CoM + methanethiol
-
 ?
2.1.1.251 dimethylsulfide + coenzyme M Methanosarcina barkeri Fusaro, DSM 804
-
 methyl-CoM + methanethiol
-
 ?
2.1.1.251 dimethylsulfide + coenzyme M Methanosarcina barkeri Fusaro / DSM 804
-
 methyl-CoM + methanethiol
-
 ?
2.1.1.251 methanethiol + coenzyme M Methanosarcina barkeri
-
 methyl-CoM + hydrogen sulfide
-
 ?
2.1.1.251 methylmercaptopropionate + coenzyme M Methanosarcina barkeri
-
 methyl-CoM + mercaptopropionate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.246 Methanosarcina barkeri
-
 DSM 804, gene mtaA
-
2.1.1.246 Methanosarcina barkeri Fusaro / DSM 804
-
 DSM 804, gene mtaA
-
2.1.1.251 Methanosarcina barkeri
-
-
-
2.1.1.251 Methanosarcina barkeri Fusaro, DSM 804
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.251 additional information methylated thiol-dependent methanogenesis in cell extract is a function of the growth substrate Methanosarcina barkeri
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.1.246 0.01
-
 purified recombinant mutant C239A MtaA, pH 7.0, 37°C Methanosarcina barkeri
2.1.1.246 0.02
-
 purified recombinant mutant H237A MtaA, pH 7.0, 37°C Methanosarcina barkeri
2.1.1.246 0.3
-
 purified recombinant wild-type MtaA, pH 7.0, 37°C Methanosarcina barkeri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.246 a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
 Methanosarcina barkeri methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
 r
2.1.1.246 a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
 Methanosarcina barkeri Fusaro, DSM 804 methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
 r
2.1.1.246 a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
 Methanosarcina barkeri Fusaro / DSM 804 methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
 r
2.1.1.251 3-methylmercapto-1-propanol + coenzyme M
-
 Methanosarcina barkeri methyl-CoM + 3-mercapto-1-propanol
-
 ?
2.1.1.251 a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M
-
 Methanosarcina barkeri methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
-
 ?
2.1.1.251 a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M
-
 Methanosarcina barkeri Fusaro, DSM 804 methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
-
 ?
2.1.1.251 a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M
-
 Methanosarcina barkeri Fusaro / DSM 804 methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
-
 ?
2.1.1.251 dimethylsulfide + coenzyme M
-
 Methanosarcina barkeri methyl-CoM + methanethiol
-
 ?
2.1.1.251 dimethylsulfide + coenzyme M
-
 Methanosarcina barkeri Fusaro, DSM 804 methyl-CoM + methanethiol
-
 ?
2.1.1.251 dimethylsulfide + coenzyme M
-
 Methanosarcina barkeri Fusaro / DSM 804 methyl-CoM + methanethiol
-
 ?
2.1.1.251 methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein]
-
 Methanosarcina barkeri a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
-
 ?
2.1.1.251 methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein]
-
 Methanosarcina barkeri Fusaro, DSM 804 a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
-
 ?
2.1.1.251 methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein]
-
 Methanosarcina barkeri Fusaro / DSM 804 a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
-
 ?
2.1.1.251 methanethiol + coenzyme M
-
 Methanosarcina barkeri methyl-CoM + hydrogen sulfide
-
 ?
2.1.1.251 methylmercaptopropionate + coenzyme M
-
 Methanosarcina barkeri methyl-CoM + mercaptopropionate
-
 r
2.1.1.251 additional information the methylthiol:CoM methyltransferase reaction is initiated only with the enzyme-bound corrinoid in the methylated state. CoM can demethylate, and dimethylsulfide and methylmercaptoproionate can remethylate, the corrinoid cofactor Methanosarcina barkeri ?
-
 ?
2.1.1.251 additional information the methylthiol:CoM methyltransferase reaction is initiated only with the enzyme-bound corrinoid in the methylated state. CoM can demethylate, and dimethylsulfide and methylmercaptoproionate can remethylate, the corrinoid cofactor Methanosarcina barkeri Fusaro, DSM 804 ?
-
 ?
2.1.1.251 additional information the methylthiol:CoM methyltransferase reaction is initiated only with the enzyme-bound corrinoid in the methylated state. CoM can demethylate, and dimethylsulfide and methylmercaptoproionate can remethylate, the corrinoid cofactor Methanosarcina barkeri Fusaro / DSM 804 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.246 methanol:coenzyme M methyltransferase
-
 Methanosarcina barkeri
2.1.1.246 mtaA
-
 Methanosarcina barkeri
2.1.1.251 480-kDa CoM methylase
-
 Methanosarcina barkeri
2.1.1.251 CoM methylase
-
 Methanosarcina barkeri
2.1.1.251 DMS:CoM methyltransferase
-
 Methanosarcina barkeri
2.1.1.251 methylthiol:CoM methyltransferase
-
 Methanosarcina barkeri
2.1.1.251 MMPA:CoM methyltransferase
-
 Methanosarcina barkeri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.246 37
-
 assay at Methanosarcina barkeri
2.1.1.251 37
-
 assay at Methanosarcina barkeri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.246 7
-
 assay at Methanosarcina barkeri
2.1.1.251 7
-
 assay at Methanosarcina barkeri

General Information

EC Number General Information Comment Organism
2.1.1.251 metabolism 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 Methanosarcina barkeri
2.1.1.251 additional information 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 Methanosarcina barkeri
2.1.1.251 physiological function 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 Methanosarcina barkeri