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Literature summary extracted from

  • Tallant, T.C.; Krzycki, J.A.
    Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of methanogenesis from dimethylsulfide and methylmercaptopropionate (1997), J. Bacteriol., 179, 6902-6911.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.1.1.251 additional information ATP (10 mM) and/or MgCl2 (12 mM) do not stimulate the MMPA:CoM methyltransferase reactions mediated by the purified enzyme Methanosarcina barkeri

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.251 10
-
 methylmercaptopropionate pH 7.0, 37°C Methanosarcina barkeri

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.251 Co3+ the enzyme obligately requires the bound methylated corrinoid cofactor for activity. Corrinoid-dependent methyltransferases cycle between methylated corrinoid in the Co(III) redox state and the highly nucleophilic, reducing, and oxygen-sensitive Co(I) state. In the Co(II) form, these methyltransferase is inactive Methanosarcina barkeri
2.1.1.251 Cobalt the enzyme obligately requires the bound methylated corrinoid cofactor for activity. Corrinoid-dependent methyltransferases cycle between methylated corrinoid in the Co(III) redox state and the highly nucleophilic, reducing, and oxygen-sensitive Co(I) state. In the Co(II) form, these methyltransferase is inactive Methanosarcina barkeri

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.251 dimethylsulfide + coenzyme M Methanosarcina barkeri the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate methyl-CoM + methanethiol
-
 ?
2.1.1.251 dimethylsulfide + coenzyme M Methanosarcina barkeri DSM 800 the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate methyl-CoM + methanethiol
-
 ?
2.1.1.251 methylmercaptopropionate + coenzyme M Methanosarcina barkeri the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate methyl-CoM + mercaptopropionate
-
 ?
2.1.1.251 methylmercaptopropionate + coenzyme M Methanosarcina barkeri DSM 800 the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate methyl-CoM + mercaptopropionate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.251 Methanosarcina barkeri
-
-
-
2.1.1.251 Methanosarcina barkeri DSM 800
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.251
-
 Methanosarcina barkeri

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.1.1.251 culture condition:acetate-grown cell
-
 Methanosarcina barkeri
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.251 dimethylsulfide + coenzyme M
-
 Methanosarcina barkeri methyl-CoM + methanethiol
-
 r
2.1.1.251 dimethylsulfide + coenzyme M the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate Methanosarcina barkeri methyl-CoM + methanethiol
-
 ?
2.1.1.251 dimethylsulfide + coenzyme M
-
 Methanosarcina barkeri DSM 800 methyl-CoM + methanethiol
-
 r
2.1.1.251 dimethylsulfide + coenzyme M the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate Methanosarcina barkeri DSM 800 methyl-CoM + methanethiol
-
 ?
2.1.1.251 methylmercaptopropionate + coenzyme M
-
 Methanosarcina barkeri methyl-CoM + mercaptopropionate
-
 r
2.1.1.251 methylmercaptopropionate + coenzyme M the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate Methanosarcina barkeri methyl-CoM + mercaptopropionate
-
 ?
2.1.1.251 methylmercaptopropionate + coenzyme M
-
 Methanosarcina barkeri DSM 800 methyl-CoM + mercaptopropionate
-
 r
2.1.1.251 methylmercaptopropionate + coenzyme M the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate Methanosarcina barkeri DSM 800 methyl-CoM + mercaptopropionate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.251 CoM methylase
-
 Methanosarcina barkeri
2.1.1.251 DMS:CoM methyltransferase
-
 Methanosarcina barkeri
2.1.1.251 methylthiol:coenzyme M 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
2.1.1.251 37
-
 assay at Methanosarcina barkeri

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.251 corrinoid the enzyme obligately requires the bound methylated corrinoid cofactor for activity. Corrinoid-dependent methyltransferases cycle between methylated corrinoid in the Co(III) redox state and the highly nucleophilic, reducing, and oxygen-sensitive Co(I) state. In the Co(II) form, these methyltransferase is inactive Methanosarcina barkeri

General Information

EC Number General Information Comment Organism
2.1.1.251 physiological function the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate Methanosarcina barkeri