2.1.1.251: methylated-thiol-coenzyme M methyltransferase

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For detailed information about methylated-thiol-coenzyme M methyltransferase, go to the full flat file.

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Synonyms

480-kDa CoM methylase, CoM methylase, DMS:CoM methyltransferase, methylthiol:coenzyme M methyltransferase, methylthiol:CoM methyltransferase, methyltransferase II, MMPA:CoM methyltransferase, MtsA

ECTree

     2 Transferases

         2.1 Transferring one-carbon groups

             2.1.1 Methyltransferases

                2.1.1.251 methylated-thiol-coenzyme M methyltransferase

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Results	in table
3	Activating Compound
20	AA Sequence
1	CAS Registry Number
2	Cloned(Commentary)
2	Cofactor
13	General Information
1	Inhibitors
5	KM Value [mM]
3	Metals/Ions
5	Molecular Weight [Da]
14	Natural Substrates/ Products (Substrates)
10	Organism
5	Pathway
2	pH Optimum
2	Purification (Commentary)
4	Reaction
6	Reference
1	Renatured (Commentary)
6	Source Tissue
1	Specific Activity [micromol/min/mg]
32	Substrates and Products (Substrate)
1	Subunits
25	Synonyms
1	Systematic Name
4	Temperature Optimum [°C]

Systematic Name

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Systematic Name on EC 2.1.1.251 - methylated-thiol-coenzyme M methyltransferase

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SYSTEMATIC NAME

IUBMB Comments

methylated-thiol:coenzyme M methyltransferase

The enzyme, which is involved in methanogenesis from methylated thiols, such as methane thiol, dimethyl sulfide, and 3-(methylsulfanyl)propanoate, catalyses two successive steps - the transfer of a methyl group from the substrate to the cobalt cofactor of a methylated-thiol-specific corrinoid protein (MtsB), and the subsequent transfer of the methyl group from the corrinoid protein to CoM. With most other methanogenesis substrates this process is carried out by two different enzymes (for example, EC 2.1.1.90, methanol---corrinoid protein Co-methyltransferase, and EC 2.1.1.246, [methyl-Co(III) methanol-specific corrinoid protein]---coenzyme M methyltransferase). The cobalt is oxidized during methylation from the Co(I) state to the Co(III) state, and is reduced back to the Co(I) form during demethylation.