Literature summary for 2.1.1.246 extracted from

Dong, M.; Gonzalez, T.; Klems, M.; Steinberg, L.; Chen, W.; Papoutsakis, E.; Bahnson, B.
In vitro methanol production from methyl coenzyme M using the Methanosarcina barkeri MtaABC protein complex (2017), Biotechnol. Prog., 33, 1243-1249 .

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Application

Application	Comment	Organism
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
synthesis	in vitro methanol production from methyl coenzyme M using the Methanosarcina barkeri MtaABC protein complex	Methanosarcina barkeri

Cloned(Commentary)

Cloned (Comment)	Organism
gene mtaA, recombinant expression as enzyme complex Methanosarcina barkeri MtaABC in Escherichia coli, recombinant expression of His-tagged MtaA in Escherichia coli	Methanosarcina barkeri

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics	Methanosarcina barkeri

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
a [methyl-Co(III) methanol-specific corrinoid protein] + CoM	Methanosarcina barkeri	-	methyl-CoM + a [Co(I) methanol-specific corrinoid protein]	-	?

Organism

Organism	UniProt	Comment	Textmining
Methanosarcina barkeri	Q48949	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His-tagged MtaA from Escherichia coli by nickel affinity chromatography, dialysis, and anion exchange chromatography	Methanosarcina barkeri

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
a [methyl-Co(III) methanol-specific corrinoid protein] + CoM	-	Methanosarcina barkeri	methyl-CoM + a [Co(I) methanol-specific corrinoid protein]	-	?
a [methyl-Co(III) methanol-specific corrinoid protein] + CoM	-	Methanosarcina barkeri	methyl-CoM + a [Co(I) methanol-specific corrinoid protein]	-	r
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	?	-	-

Subunits

Subunits	Comment	Organism
?	x * 36000, recombinant His-tagged MtaA, SDS-PAGE	Methanosarcina barkeri

Synonyms

Synonyms	Comment	Organism
mtaA	-	Methanosarcina barkeri

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.2	-	assay at	Methanosarcina barkeri

General Information

General Information	Comment	Organism
additional information	enzyme complex structure analysis and structure-function analysis, overview	Methanosarcina barkeri
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

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Release 2023.1 (January 2023)