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Literature summary extracted from

  • Sauer, K.; Thauer, R.K.
    Methyl-coenzyme M formation in methanogenic archaea. Involvement of zinc in coenzyme M activation (2000), Eur. J. Biochem., 267, 2498-2504.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.246 overexpression of His-tagged inactive MtaA apoprotein in Escherichia coli strain M15 grown in the presence of 2 mM EDTA Methanosarcina barkeri

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.1.1.246 EDTA 75% inhibition at 1 mM, complete inhibition at 2 mM, reversible by Zn2+ addition, competitive versus Zn2+, kinetics, overview Methanosarcina barkeri
2.1.1.246 additional information 1 mm nitrilotriacetic acid has almost no effect on the MtaA activity Methanosarcina barkeri

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.1.1.246 Co2+ required, the apoprotein reacts with zinc or cobalt to the fully active holoenzyme Methanosarcina barkeri
2.1.1.246 additional information Zn21 or Co21 are required for MtaA activity, Zn2+ can be replaced by Co2+ but not by Mg2+, the kinetics of activation by Co2+ being similarily slow. About 1 mol of transition metal is bound per mol of protein. The role of the transition metal in MtaA is to lower the microscopic pKa of the thiol group of coenzyme M by coordination to the zinc, and thus to increase its nucleophilicity for methyl group attack, pKZn2+ of MtaA is over 15 Methanosarcina barkeri
2.1.1.246 Zn2+ 1 mol per mol of enzyme, required, the apoprotein reacts with zinc or cobalt to the fully active holoenzyme Methanosarcina barkeri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.1.1.246 50000
-
 x * 50000 Methanosarcina barkeri

Natural Substrates/ Products (Substrates)

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]
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.246 Methanosarcina barkeri
-
 gene mtaA
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.1.1.246 recombinant His-tagged apo MtaA from Escherichia coli strain M15 by nickel affinity and anionexchange chromatography Methanosarcina barkeri

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.246 a [methyl-Co(III) methanol-specific corrinoid protein] + CoM = methyl-CoM + a [Co(I) methanol-specific corrinoid protein] coenzyme M binds with its thiol group to the zinc in the active site of MtaA forming a coenzyme M thiolate zinc complex Methanosarcina barkeri
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.1.1.246 2
-
 purified Zn2+-containing holoenzyme, pH 7.0, 37°C Methanosarcina barkeri

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) 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]
-
 ?

Subunits

EC Number Subunits Comment Organism
2.1.1.246 ? x * 50000 Methanosarcina barkeri

Synonyms

EC Number Synonyms Comment Organism
2.1.1.246 mtaA
-
 Methanosarcina barkeri

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.1.1.246 37
-
 assay at Methanosarcina barkeri

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.1.1.246 7
-
 assay at Methanosarcina barkeri

General Information

EC Number General Information Comment Organism
2.1.1.246 additional information MtaC and MtaB form a tight complex and the encoding genes form a transcription unit, whereas MtaA purifies separately and its encoding gene is located separately Methanosarcina barkeri
2.1.1.246 physiological function the methyltransferase designated MtaA together with the proteins MtaB and MtaC mediate the formation of methyl-coenzyme M from methanol and coenzyme M. MtaC is a 28-kDa corrinoid protein, MtaB, EC 2.1.1.90, catalyzes the methylation of MtaC and MtaA catalyzes the demethylation of methylated MtaC Methanosarcina barkeri