EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.1.246 | genes cmtA and cmtM, DNA and amino acid sequence determination and analysis, expressionin Escherichia coli strain XL-1 Blue | Methanosarcina barkeri |
2.1.1.247 | genes cmtA and cmtM, DNA and amino acid sequence determination and analysis, expression of the isozymes in Escherichia coli | Methanosarcina barkeri |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.247 | 1,10-phenanthroline | - |
Methanosarcina barkeri | |
2.1.1.247 | EDTA | - |
Methanosarcina barkeri | |
2.1.1.247 | EGTA | - |
Methanosarcina barkeri |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.1.1.246 | additional information | - |
additional information | steady-state kinetics of isozymes MT2-A and MT2-M, overview | Methanosarcina barkeri | |
2.1.1.247 | additional information | - |
additional information | steady-state kinetics | Methanosarcina barkeri | |
2.1.1.247 | 0.000014 | - |
[methyl-Co(III) trimethylamine-specific corrinoid protein] | isozymes MT2-A and MT-2-M, pH 7.2, 23°C | Methanosarcina barkeri | |
2.1.1.247 | 0.02 | - |
coenzyme M | isozyme MT2-M, pH 7.2, 23°C | Methanosarcina barkeri | |
2.1.1.247 | 0.035 | - |
coenzyme M | isozyme MT2-A, pH 7.2, 23°C | Methanosarcina barkeri | |
2.1.1.247 | 9 | - |
3-Mercaptopropionate | isozyme MT2-A, pH 7.2, 23°C | Methanosarcina barkeri | |
2.1.1.247 | 10 | - |
3-Mercaptopropionate | isozyme MT2-M, pH 7.2, 23°C | Methanosarcina barkeri |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.246 | Zn2+ | - |
Methanosarcina barkeri | |
2.1.1.247 | Zn2+ | both isozymes are zinc-containing metalloproteins, zinc involvement in catalysis of coenzyme M methylation | Methanosarcina barkeri |
EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
2.1.1.246 | 34000 | - |
x * 34000, isozymes MT2-A and MT2-M, SDS-PAGE, x * 36700, about, isozyme MT2-A, sequence calculation | Methanosarcina barkeri |
2.1.1.246 | 36700 | - |
x * 34000, isozymes MT2-A and MT2-M, SDS-PAGE, x * 36700, about, isozyme MT2-A, sequence calculation | Methanosarcina barkeri |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.246 | a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M | Methanosarcina barkeri | - |
methyl-CoM + a [Co(I) methanol-specific corrinoid protein] | - |
r | |
2.1.1.246 | additional information | Methanosarcina barkeri | conversions of monomethylamine and dimethylamine to CH3-SCoM are dependent upon MT2-A, and are not supported by MT2-M. In contrast, MT2-M acts specifically in metabolism of methanol, but does not substitute for MT2-A in conversion of monomethylamine or dimethylamine. Nevertheless, both isozymes are capable of supporting the conversion of trimethylamine | ? | - |
? | |
2.1.1.247 | HSCoM + methylcobalamin | Methanosarcina barkeri | - |
CH3-SCoM + cob(I)alamin + H+ | - |
r | |
2.1.1.247 | [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 |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.246 | Methanosarcina barkeri | O30640 | isozymes MT2-A and MT2-M encoded by genes cmtA and cmtM | - |
2.1.1.247 | Methanosarcina barkeri | O30640 | isozymes MT2-A and MT2-M encoded by genes cmtA and cmtM | - |
EC Number | Source Tissue | Comment | Organism | Textmining |
---|---|---|---|---|
2.1.1.246 | cell culture | the isozymes MT2-A and MT2-M are differentially expressed depending upon the substrate available for growth | Methanosarcina barkeri | - |
EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|---|
2.1.1.246 | 0.154 | - |
MT2 activity in recombinant Escherichia coli cells transfected with gene cmtM, pH 7.2, 37°C | Methanosarcina barkeri |
2.1.1.246 | 1.21 | - |
MT2 activity in recombinant Escherichia coli cells transfected with gene cmtA, pH 7.2, 37°C | Methanosarcina barkeri |
2.1.1.246 | 2.2 | - |
MT2 activity in cells grown on trimethylamine, pH 7.2, 37°C | Methanosarcina barkeri |
2.1.1.246 | 7.5 | - |
MT2 activity in cells grown on methanol, pH 7.2, 37°C | Methanosarcina barkeri |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.246 | a [methyl-Co(III) methanol-specific corrinoid protein] + 3-mercaptopropanoic acid | - |
Methanosarcina barkeri | methyl-3-mercaptopropanoic acid + a [Co(I) methanol-specific corrinoid protein] | - |
r | |
2.1.1.246 | a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M | - |
Methanosarcina barkeri | methyl-CoM + a [Co(I) methanol-specific corrinoid protein] | - |
r | |
2.1.1.246 | a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M | the enzyme methylcobamide:CoM methyltransferase, MT2, catalyzes the transfer of the methyl group from the MT1-bound methylcobamide prosthetic group to coenzyme M | Methanosarcina barkeri | methyl-CoM + a [Co(I) methanol-specific corrinoid protein] | - |
r | |
2.1.1.246 | additional information | conversions of monomethylamine and dimethylamine to CH3-SCoM are dependent upon MT2-A, and are not supported by MT2-M. In contrast, MT2-M acts specifically in metabolism of methanol, but does not substitute for MT2-A in conversion of monomethylamine or dimethylamine. Nevertheless, both isozymes are capable of supporting the conversion of trimethylamine | Methanosarcina barkeri | ? | - |
? | |
2.1.1.247 | HSCoM + methylcobalamin | - |
Methanosarcina barkeri | CH3-SCoM + cob(I)alamin + H+ | - |
r | |
2.1.1.247 | 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 | ? | - |
? | |
2.1.1.247 | [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 | |
2.1.1.247 | [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 | |
2.1.1.247 | [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] | - |
? | |
2.1.1.247 | [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 | |
2.1.1.247 | [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 |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.1.246 | ? | x * 34000, isozymes MT2-A and MT2-M, SDS-PAGE, x * 36700, about, isozyme MT2-A, sequence calculation | Methanosarcina barkeri |
2.1.1.246 | More | the isozymes MT2-A and MT2-M differ in their overall charge | Methanosarcina barkeri |
2.1.1.247 | ? | x * 36000-37000, recombinant isozymes MT2-A and MT2-M, SDS-PAGE | Methanosarcina barkeri |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.1.246 | methylcobamide:coenzyme M methyltransferase | - |
Methanosarcina barkeri |
2.1.1.246 | methylcobamide:CoM methyltransferase | - |
Methanosarcina barkeri |
2.1.1.246 | MT2-A | - |
Methanosarcina barkeri |
2.1.1.246 | MT2-M | - |
Methanosarcina barkeri |
2.1.1.247 | methylcobamide:coenzyme M methyltransferase | - |
Methanosarcina barkeri |
2.1.1.247 | MT2 | - |
Methanosarcina barkeri |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.1.246 | 37 | - |
assay at | Methanosarcina barkeri |
2.1.1.247 | 23 | - |
assay at | Methanosarcina barkeri |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.1.1.246 | 7.2 | - |
assay at | Methanosarcina barkeri |
2.1.1.247 | 7.2 | - |
assay at | Methanosarcina barkeri |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.247 | additional information | no enzyme-bound organic or inorganic cofactors | Methanosarcina barkeri |
EC Number | IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|---|
2.1.1.247 | 0.005 | - |
pH 7.2, 23°C | Methanosarcina barkeri | EDTA | |
2.1.1.247 | 0.05 | - |
pH 7.2, 23°C | Methanosarcina barkeri | EGTA | |
2.1.1.247 | 0.07 | - |
pH 7.2, 23°C | Methanosarcina barkeri | 1,10-phenanthroline |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.1.1.247 | 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 |