Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Cobalt | the enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP | Methanosarcina barkeri | |
Iron | presence of 1.7 mol of non-heme iron per mol of enzyme | Methanosarcina barkeri | |
Mg2+ | plays a role in binding of the corrinoid prosthetic group and in subunit association | Methanosarcina barkeri |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
121000 | - |
gradient PAGE, gel filtration | Methanosarcina barkeri |
122000 | - |
gel filtration | Methanosarcina barkeri |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
methanol + a [Co(I) methanol-specific corrinoid protein] | Methanosarcina barkeri | first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme | a [methyl-Co(III) methanol-specific corrinoid protein] + H2O | - |
? | |
methanol + a [Co(I) methanol-specific corrinoid protein] | Methanosarcina barkeri DSM 800 | first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme | a [methyl-Co(III) methanol-specific corrinoid protein] + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanosarcina barkeri | - |
- |
- |
Methanosarcina barkeri DSM 800 | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Methanosarcina barkeri |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
methanol + a [Co(I) methanol-specific corrinoid protein] | - |
Methanosarcina barkeri | a [methyl-Co(III) methanol-specific corrinoid protein] + H2O | - |
? | |
methanol + a [Co(I) methanol-specific corrinoid protein] | first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme | Methanosarcina barkeri | a [methyl-Co(III) methanol-specific corrinoid protein] + H2O | - |
? | |
methanol + a [Co(I) methanol-specific corrinoid protein] | - |
Methanosarcina barkeri DSM 800 | a [methyl-Co(III) methanol-specific corrinoid protein] + H2O | - |
? | |
methanol + a [Co(I) methanol-specific corrinoid protein] | first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme | Methanosarcina barkeri DSM 800 | a [methyl-Co(III) methanol-specific corrinoid protein] + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
methanol:5-hydroxybenzimidazolylcobamide methyltransferase | - |
Methanosarcina barkeri |
MT1 | - |
Methanosarcina barkeri |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Methanosarcina barkeri |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Methanosarcina barkeri |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
corrinoid | the enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme | Methanosarcina barkeri |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Methanosarcina barkeri | isoelectric focusing | - |
4.5 |
General Information | Comment | Organism |
---|---|---|
physiological function | first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in Methanosarcina barkeri | Methanosarcina barkeri |