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Literature summary for 2.1.1.251 extracted from
- 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.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | ATP and/or MgCl2 do not stimulate the MMPA:CoM methyltransferase reactions mediated by the purified methylthiol: CoM methyltransferase | Methanosarcina barkeri | |
| Ti(III) citrate | not essential activation | Methanosarcina barkeri |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 480000 | - |
- |
Methanosarcina barkeri |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| dimethylsulfide + coenzyme M | Methanosarcina barkeri | - |
methyl-CoM + methanethiol | - |
? | |
| dimethylsulfide + coenzyme M | Methanosarcina barkeri Fusaro, DSM 804 | - |
methyl-CoM + methanethiol | - |
? | |
| dimethylsulfide + coenzyme M | Methanosarcina barkeri Fusaro / DSM 804 | - |
methyl-CoM + methanethiol | - |
? | |
| methanethiol + coenzyme M | Methanosarcina barkeri | - |
methyl-CoM + hydrogen sulfide | - |
? | |
| methylmercaptopropionate + coenzyme M | Methanosarcina barkeri | - |
methyl-CoM + mercaptopropionate | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanosarcina barkeri | - |
- |
- |
| Methanosarcina barkeri Fusaro, DSM 804 | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| additional information | methylated thiol-dependent methanogenesis in cell extract is a function of the growth substrate | Methanosarcina barkeri | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 3-methylmercapto-1-propanol + coenzyme M | - |
Methanosarcina barkeri | methyl-CoM + 3-mercapto-1-propanol | - |
? | |
| a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M | - |
Methanosarcina barkeri | methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein] | - |
? | |
| 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] | - |
? | |
| 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] | - |
? | |
| dimethylsulfide + coenzyme M | - |
Methanosarcina barkeri | methyl-CoM + methanethiol | - |
? | |
| dimethylsulfide + coenzyme M | - |
Methanosarcina barkeri Fusaro, DSM 804 | methyl-CoM + methanethiol | - |
? | |
| dimethylsulfide + coenzyme M | - |
Methanosarcina barkeri Fusaro / DSM 804 | methyl-CoM + methanethiol | - |
? | |
| methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein] | - |
Methanosarcina barkeri | a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide | - |
? | |
| 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 | - |
? | |
| 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 | - |
? | |
| methanethiol + coenzyme M | - |
Methanosarcina barkeri | methyl-CoM + hydrogen sulfide | - |
? | |
| methylmercaptopropionate + coenzyme M | - |
Methanosarcina barkeri | methyl-CoM + mercaptopropionate | - |
r | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| 480-kDa CoM methylase | - |
Methanosarcina barkeri |
| CoM methylase | - |
Methanosarcina barkeri |
| DMS:CoM 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 |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Methanosarcina barkeri |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 |
| 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 |
| 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 |
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