Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
additional information | analysis of the metal content of MtbB1 by plasma emission spectroscopy revealed no detectable cobalt with a lower limit of detection for cobalt of 0.04 mol of cobalt/mol of polypeptide | Methanosarcina barkeri | |
Zn2+ | 0.43 mol of zinc/mol of polypeptide | Methanosarcina barkeri |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
51000 | - |
x * 51000, SDS-PAGE | Methanosarcina barkeri |
230000 | - |
gel filtration | Methanosarcina barkeri |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein] | Methanosarcina barkeri | - |
a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine | - |
? | |
additional information | Methanosarcina barkeri | MtbB1 demethylates dimethylamine and specifically methylates the corrinoid prosthetic group of MtbC, which is subsequently demethylated by MtbA to methylate coenzyme M during methanogenesis from dimethylamine. A MtbB1to corrinoid protein MtbC ratio of 1 is optimal for coenzyme M methylation with dimethylamine. MtbB1 methylated either corrinoid bound to MtbC or free cob(I)alamin with dimethylamine, indicating MtbB1 carries an active site for dimethylamine demethylation and corrinoid methylation | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Methanosarcina barkeri | - |
gene mtbB1 | - |
Purification (Comment) | Organism |
---|---|
native enzyme 35.2fold MtbB1 by two steps of anion exchange chromatography, and adsorption and hydrophobic interaction chromatography | Methanosarcina barkeri |
Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
1.89 | - |
purified enzyme, pH 6.5, 23°C | Methanosarcina barkeri |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
dimethylamine + a [Co(I) dimethylamine-specific corrinoid protein] | - |
Methanosarcina barkeri | a [methyl-Co(III) dimethylamine-specific corrinoid protein] + methylamine | - |
? | |
additional information | MtbB1 demethylates dimethylamine and specifically methylates the corrinoid prosthetic group of MtbC, which is subsequently demethylated by MtbA to methylate coenzyme M during methanogenesis from dimethylamine. A MtbB1to corrinoid protein MtbC ratio of 1 is optimal for coenzyme M methylation with dimethylamine. MtbB1 methylated either corrinoid bound to MtbC or free cob(I)alamin with dimethylamine, indicating MtbB1 carries an active site for dimethylamine demethylation and corrinoid methylation | Methanosarcina barkeri | ? | - |
? | |
additional information | dimethylamine-dependent methylation of free cobalamin by MtbB1, kinetics, overview | Methanosarcina barkeri | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
oligomer | x * 51000, SDS-PAGE | Methanosarcina barkeri |
Synonyms | Comment | Organism |
---|---|---|
dimethylamine: corrinoid methyltransferase | - |
Methanosarcina barkeri |
DMA:corrinoid methyltransferase | - |
Methanosarcina barkeri |
MtbB1 | - |
Methanosarcina barkeri |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
23 | - |
assay at | Methanosarcina barkeri |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
assay at | Methanosarcina barkeri |
General Information | Comment | Organism |
---|---|---|
metabolism | highly purified dimethylamine: corrinoid methyltransferase MtbB1, corrinoid protein MtbC, and methylcorrinoid:coenzyme M methyltransferase MtbA, EC 2.1.1.247, are sufficient to catalyze in vitro CoM methylation by DMA | Methanosarcina barkeri |
additional information | MtbB1 is a 230-kDa protein composed of 51-kDa subunits that do not possess a corrinoid prosthetic group | Methanosarcina barkeri |