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Literature summary for 2.1.1.251 extracted from
- Methylthiol:coenzyme M methyltransferase from Methanosarcina barkeri, an enzyme of methanogenesis from dimethylsulfide and methylmercaptopropionate (1997), J. Bacteriol., 179, 6902-6911.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| 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]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 10 | - |
methylmercaptopropionate | pH 7.0, 37°C | Methanosarcina barkeri |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| 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 | |
| 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]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 480000 | - |
gel filtration | Methanosarcina barkeri |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dimethylsulfide + coenzyme M | Methanosarcina barkeri | the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate | methyl-CoM + methanethiol | - |
? | |
| dimethylsulfide + coenzyme M | Methanosarcina barkeri DSM 800 | the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate | methyl-CoM + methanethiol | - |
? | |
| methylmercaptopropionate + coenzyme M | Methanosarcina barkeri | the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate | methyl-CoM + mercaptopropionate | - |
? | |
| methylmercaptopropionate + coenzyme M | Methanosarcina barkeri DSM 800 | the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate | methyl-CoM + mercaptopropionate | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanosarcina barkeri | - |
- |
- |
| Methanosarcina barkeri DSM 800 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Methanosarcina barkeri |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| culture condition:acetate-grown cell | - |
Methanosarcina barkeri | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dimethylsulfide + coenzyme M | - |
Methanosarcina barkeri | methyl-CoM + methanethiol | - |
r | |
| dimethylsulfide + coenzyme M | the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate | Methanosarcina barkeri | methyl-CoM + methanethiol | - |
? | |
| dimethylsulfide + coenzyme M | - |
Methanosarcina barkeri DSM 800 | methyl-CoM + methanethiol | - |
r | |
| dimethylsulfide + coenzyme M | the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate | Methanosarcina barkeri DSM 800 | methyl-CoM + methanethiol | - |
? | |
| methylmercaptopropionate + coenzyme M | - |
Methanosarcina barkeri | methyl-CoM + mercaptopropionate | - |
r | |
| methylmercaptopropionate + coenzyme M | the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate | Methanosarcina barkeri | methyl-CoM + mercaptopropionate | - |
? | |
| methylmercaptopropionate + coenzyme M | - |
Methanosarcina barkeri DSM 800 | methyl-CoM + mercaptopropionate | - |
r | |
| methylmercaptopropionate + coenzyme M | the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate | Methanosarcina barkeri DSM 800 | methyl-CoM + mercaptopropionate | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CoM methylase | - |
Methanosarcina barkeri |
| DMS:CoM methyltransferase | - |
Methanosarcina barkeri |
| methylthiol:coenzyme M methyltransferase | - |
Methanosarcina barkeri |
| methylthiol:CoM methyltransferase | - |
Methanosarcina barkeri |
| MMPA:CoM methyltransferase | - |
Methanosarcina barkeri |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Methanosarcina barkeri |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| 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
| General Information | Comment | Organism |
|---|---|---|
| physiological function | the enzyme functions as a CoM methylase during methanogenesis from dimethylsulfide or methylmercaptopropionate | Methanosarcina barkeri |
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