EC Number | Application | Comment | Organism |
---|---|---|---|
2.1.1.246 | biofuel production | demonstration of an in vitro ability of MtaABC to produce methanol may ultimately enable the anaerobic oxidation of methane to produce methanol and from methanol alternative fuel or fuel-precursor molecules | Methanosarcina barkeri |
2.1.1.246 | synthesis | in vitro methanol production from methyl coenzyme M using the Methanosarcina barkeri MtaABC protein complex | Methanosarcina barkeri |
EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.1.90 | expressed in Escherichia coli BL21 cells | Methanosarcina barkeri |
2.1.1.246 | gene mtaA, recombinant expression as enzyme complex Methanosarcina barkeri MtaABC in Escherichia coli, recombinant expression of His-tagged MtaA in Escherichia coli | Methanosarcina barkeri |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
2.1.1.246 | additional information | - |
additional information | kinetics | Methanosarcina barkeri |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.90 | methanol + cob(I)alamin | Methanosarcina barkeri | - |
methyl-cob(III)alamin + H2O | - |
r | |
2.1.1.90 | methanol + cob(I)alamin | Methanosarcina barkeri DSM 804 | - |
methyl-cob(III)alamin + H2O | - |
r | |
2.1.1.246 | a [methyl-Co(III) methanol-specific corrinoid protein] + CoM | Methanosarcina barkeri | - |
methyl-CoM + a [Co(I) methanol-specific corrinoid protein] | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.90 | Methanosarcina barkeri | Q48949 and Q46EH3 and Q46EH4 | subunits MtaA and MtaB and MtaC | - |
2.1.1.90 | Methanosarcina barkeri DSM 804 | Q48949 and Q46EH3 and Q46EH4 | subunits MtaA and MtaB and MtaC | - |
2.1.1.246 | Methanosarcina barkeri | Q48949 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
2.1.1.90 | Ni-NTA column chromatography and Q Sepharose column chromatography | Methanosarcina barkeri |
2.1.1.246 | recombinant His-tagged MtaA from Escherichia coli by nickel affinity chromatography, dialysis, and anion exchange chromatography | Methanosarcina barkeri |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.90 | methanol + cob(I)alamin | - |
Methanosarcina barkeri | methyl-cob(III)alamin + H2O | - |
r | |
2.1.1.90 | methanol + cob(I)alamin | - |
Methanosarcina barkeri DSM 804 | methyl-cob(III)alamin + H2O | - |
r | |
2.1.1.246 | a [methyl-Co(III) methanol-specific corrinoid protein] + CoM | - |
Methanosarcina barkeri | methyl-CoM + a [Co(I) methanol-specific corrinoid protein] | - |
? | |
2.1.1.246 | a [methyl-Co(III) methanol-specific corrinoid protein] + CoM | - |
Methanosarcina barkeri | methyl-CoM + a [Co(I) methanol-specific corrinoid protein] | - |
r | |
2.1.1.246 | additional information | the reaction for possible production of methanol from the anaerobic oxidation of methane can be reversed in vitro. Develoment of an in vitro functional assay that demonstrates MtaABC can catalyze the energetically unfavorable reverse reaction starting from methyl coenzyme M and generating methanol as a product, overview. MtaABC enzyme protein complex to catalyze the methyl transfer from methanol to CoM to form methyl-CoM, which is energetically favorable in the forward reaction. MtaB catalyzes a methyl transfer from methanol to the corrinoid cofactor of the MtaC subunit. MtaA then catalyzes the transfer of the methyl group to CoM to form methyl-CoM. DTNB assays for the forward and reverse MtaABC reactions. Methylcobalamin assay of purified recombinant MtaA.Demethylation of methylcobalamin in a CoM-dependent manner by MtaA | Methanosarcina barkeri | ? | - |
- |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.1.90 | ? | x * 49000 + x * 36000 + x * 24000, SDS-PAGE | Methanosarcina barkeri |
2.1.1.246 | ? | x * 36000, recombinant His-tagged MtaA, SDS-PAGE | Methanosarcina barkeri |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.1.90 | methanol:coenzyme M methyltransferase | - |
Methanosarcina barkeri |
2.1.1.90 | methanol:CoM methyltransferase complex | - |
Methanosarcina barkeri |
2.1.1.90 | MtaABC | - |
Methanosarcina barkeri |
2.1.1.246 | mtaA | - |
Methanosarcina barkeri |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.1.1.246 | 7.2 | - |
assay at | Methanosarcina barkeri |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.1.1.246 | additional information | enzyme complex structure analysis and structure-function analysis, overview | Methanosarcina barkeri |
2.1.1.246 | physiological function | methanol:coenzyme M methyltransferase is an enzyme complex composed of three subunits, MtaA, MtaB, and MtaC, found in methanogenic archaea and is needed for their growth on methanol ultimately producing methane. MtaABC catalyzes the energetically favorable methyl transfer from methanol to coenzyme M to form methyl coenzyme M, an important reaction for possible production of methanol from the anaerobic oxidation of methane | Methanosarcina barkeri |