Cloned (Comment) | Organism |
---|---|
genes cmtA and cmtM, DNA and amino acid sequence determination and analysis, expression of the isozymes in Escherichia coli | Methanosarcina barkeri |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
1,10-phenanthroline | - |
Methanosarcina barkeri | |
EDTA | - |
Methanosarcina barkeri | |
EGTA | - |
Methanosarcina barkeri |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics | Methanosarcina barkeri | |
0.000014 | - |
[methyl-Co(III) trimethylamine-specific corrinoid protein] | isozymes MT2-A and MT-2-M, pH 7.2, 23°C | Methanosarcina barkeri | |
0.02 | - |
coenzyme M | isozyme MT2-M, pH 7.2, 23°C | Methanosarcina barkeri | |
0.035 | - |
coenzyme M | isozyme MT2-A, pH 7.2, 23°C | Methanosarcina barkeri | |
9 | - |
3-Mercaptopropionate | isozyme MT2-A, pH 7.2, 23°C | Methanosarcina barkeri | |
10 | - |
3-Mercaptopropionate | isozyme MT2-M, pH 7.2, 23°C | Methanosarcina barkeri |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | both isozymes are zinc-containing metalloproteins, zinc involvement in catalysis of coenzyme M methylation | Methanosarcina barkeri |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
HSCoM + methylcobalamin | Methanosarcina barkeri | - |
CH3-SCoM + cob(I)alamin + H+ | - |
r | |
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M | Methanosarcina barkeri | heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction | methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein] | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanosarcina barkeri | O30640 | isozymes MT2-A and MT2-M encoded by genes cmtA and cmtM | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
HSCoM + methylcobalamin | - |
Methanosarcina barkeri | CH3-SCoM + cob(I)alamin + H+ | - |
r | |
additional information | conversions of monomethylamine and dimethylamine to CH3-SCoM are dependent upon MT2-A, and are not supported by MT2-M, both isozymes catalyze S-methylation of 2-thioethanesulfonate, i.e. coenzyme M, and exhibit similar apparent Km values for coenzyme M, isozymes substrate specificities, overview | Methanosarcina barkeri | ? | - |
? | |
[methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M | isozyme MT2-A, not MT2-M | Methanosarcina barkeri | methyl-CoM + [Co(I) dimethylamine-specific corrinoid protein] | - |
r | |
[methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M | isozyme MT2-A, not MT2-M | Methanosarcina barkeri | methyl-CoM + [Co(I) monomethylamine-specific corrinoid protein] | - |
r | |
[methyl-Co(III) trimethylamine-specific corrinoid protein] + 3-mercaptopropionate | 3-mercaptopropionate is a coenzyme M analogue | Methanosarcina barkeri | methyl-3-mercaptopropionate + [Co(I) trimethylamine-specific corrinoid protein] | - |
? | |
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M | heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction | Methanosarcina barkeri | methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein] | - |
r | |
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M | isozymes MT2-A and MT2-M, heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction | Methanosarcina barkeri | methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein] | - |
r |
Subunits | Comment | Organism |
---|---|---|
? | x * 36000-37000, recombinant isozymes MT2-A and MT2-M, SDS-PAGE | Methanosarcina barkeri |
Synonyms | Comment | Organism |
---|---|---|
methylcobamide:coenzyme M methyltransferase | - |
Methanosarcina barkeri |
MT2 | - |
Methanosarcina barkeri |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
23 | - |
assay at | Methanosarcina barkeri |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.2 | - |
assay at | Methanosarcina barkeri |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | no enzyme-bound organic or inorganic cofactors | Methanosarcina barkeri |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
0.005 | - |
pH 7.2, 23°C | Methanosarcina barkeri | EDTA | |
0.05 | - |
pH 7.2, 23°C | Methanosarcina barkeri | EGTA | |
0.07 | - |
pH 7.2, 23°C | Methanosarcina barkeri | 1,10-phenanthroline |
General Information | Comment | Organism |
---|---|---|
additional information | the enzyme shows an active site geometry in which coenzyme M is bound both by S-coordination to zinc, and electrostatic interaction of the sulfonate with a cationic group on the enzyme | Methanosarcina barkeri |