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Literature summary for 2.1.1.246 extracted from
- Methyl-coenzyme M formation in methanogenic archaea. Involvement of zinc in coenzyme M activation (2000), Eur. J. Biochem., 267, 2498-2504.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression of His-tagged inactive MtaA apoprotein in Escherichia coli strain M15 grown in the presence of 2 mM EDTA | Methanosarcina barkeri |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| EDTA | 75% inhibition at 1 mM, complete inhibition at 2 mM, reversible by Zn2+ addition, competitive versus Zn2+, kinetics, overview | Methanosarcina barkeri |  |
| additional information | 1 mm nitrilotriacetic acid has almost no effect on the MtaA activity | Methanosarcina barkeri |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | required, the apoprotein reacts with zinc or cobalt to the fully active holoenzyme | Methanosarcina barkeri | |
| additional information | Zn21 or Co21 are required for MtaA activity, Zn2+ can be replaced by Co2+ but not by Mg2+, the kinetics of activation by Co2+ being similarily slow. About 1 mol of transition metal is bound per mol of protein. The role of the transition metal in MtaA is to lower the microscopic pKa of the thiol group of coenzyme M by coordination to the zinc, and thus to increase its nucleophilicity for methyl group attack, pKZn2+ of MtaA is over 15 | Methanosarcina barkeri | |
| Zn2+ | 1 mol per mol of enzyme, required, the apoprotein reacts with zinc or cobalt to the fully active holoenzyme | Methanosarcina barkeri | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 50000 | - |
x * 50000 | Methanosarcina barkeri |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M | Methanosarcina barkeri | - |
methyl-CoM + a [Co(I) methanol-specific corrinoid protein] | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Methanosarcina barkeri | - |
gene mtaA | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged apo MtaA from Escherichia coli strain M15 by nickel affinity and anionexchange chromatography | Methanosarcina barkeri |
Reaction
| Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|
| a [methyl-Co(III) methanol-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methanol-specific corrinoid protein] | coenzyme M binds with its thiol group to the zinc in the active site of MtaA forming a coenzyme M thiolate zinc complex | Methanosarcina barkeri |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 2 | - |
purified Zn2+-containing holoenzyme, pH 7.0, 37°C | Methanosarcina barkeri |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M | - |
Methanosarcina barkeri | methyl-CoM + a [Co(I) methanol-specific corrinoid protein] | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 50000 | Methanosarcina barkeri |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| mtaA | - |
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 |
|---|---|---|
| additional information | MtaC and MtaB form a tight complex and the encoding genes form a transcription unit, whereas MtaA purifies separately and its encoding gene is located separately | Methanosarcina barkeri |
| physiological function | the methyltransferase designated MtaA together with the proteins MtaB and MtaC mediate the formation of methyl-coenzyme M from methanol and coenzyme M. MtaC is a 28-kDa corrinoid protein, MtaB, EC 2.1.1.90, catalyzes the methylation of MtaC and MtaA catalyzes the demethylation of methylated MtaC | Methanosarcina barkeri |
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Release 2023.1 (January 2023)
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