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Literature summary for 2.1.1.247 extracted from
- Zinc-thiolate intermediate in catalysis of methyl group transfer in Methanosarcina barkeri (2001), Biochemistry, 40, 13068-13078.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene mtbA, isozyme MT2-A, DNA and amino acid sequence determination and analysis, expression as His6-tagged enzyme in Escherichia coli strain M15 | Methanosarcina barkeri |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | strong inhibition of both isozymes MT2-A and MT2-M | Methanosarcina barkeri |  |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | reconstitution of apo-enzyme with Co2+ yields an enzyme with 16fold higher specific activity, cysteine thiolate coordination in approximate tetrahedral geometry indicated by strong d-d transition absorbance centered at 622 nm, overview | Methanosarcina barkeri | |
| Zn2+ | required for activity by both isozymes MT2-A and MT2-M, tightly bound by the enzyme, 0.63 mol of Zn/mol of MT2-A, can be substituted by Co2+, which results in 16fold higher activity. Zn2+-MT2-A reveals 2S + 2N/O coordination with evidence for involvement of histidine. Interaction with the substrate CoM (2-mercaptoethanesulfonic acid) results in replacement of the second N/O group with S, indicating direct coordination of the CoM thiolate. Additional formation of an additional metal-thiolate bond, overview. Model formation in which metalthiolate formation occurs separately from H+ release from the enzyme-substrate complex at pH 6.2-7.7 | Methanosarcina barkeri | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanosarcina barkeri | O30640 | isozymes MT2-A and MT2-M, gene mtbA | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His6-tagged isozyme MT2-A from Escherichia coli strain M15 by anion exchange and hydrophobic interaction chromatography, and ultrafiltration to approximately 98% purity | Methanosarcina barkeri |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| a [methyl-Co(III) methylamine-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methylamine-specific corrinoid protein] | catalysis by MT2 proceeds by nucleophilic substitution, with attack of CoM on the methylcorrinoid Co3+-methyl group and expulsion of the demethylated corrinoid in the Co1+ form | Methanosarcina barkeri |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| a [methyl-Co(III) methylamine-specific corrinoid protein] + coenzyme M | binding analysis of CoM at the metal center of isozyme MT2-A, overview | Methanosarcina barkeri | methyl-CoM + a [Co(I) methylamine-specific corrinoid protein] | - |
? | |
| additional information | the enzyme exhibits MT2 activity, the MT2 activity is measured by following the coenzyme-M-dependent demethylation of methylcobalamin. Trimethylammonium:coenzyme M methyltransferase activity detected by coenzyme M methylation | Methanosarcina barkeri | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| methylcobamide:CoM methyltransferase | - |
Methanosarcina barkeri |
| methyltransferase 2 | - |
Methanosarcina barkeri |
| MT2 | - |
Methanosarcina barkeri |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Methanosarcina barkeri |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.2 | - |
assay at | Methanosarcina barkeri |
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Release 2023.1 (January 2023)
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