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Literature summary for 2.1.1.247 extracted from

  • LeClerc, G.M.; Grahame, D.A.
    Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression (1996), J. Biol. Chem., 271, 18725-18731.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
genes cmtA and cmtM, DNA and amino acid sequence determination and analysis, expression of the isozymes in Escherichia coli Methanosarcina barkeri

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline
-
Methanosarcina barkeri
EDTA
-
Methanosarcina barkeri
EGTA
-
Methanosarcina barkeri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information steady-state kinetics Methanosarcina barkeri
0.000014
-
[methyl-Co(III) trimethylamine-specific corrinoid protein] isozymes MT2-A and MT-2-M, pH 7.2, 23°C Methanosarcina barkeri
0.02
-
coenzyme M isozyme MT2-M, pH 7.2, 23°C Methanosarcina barkeri
0.035
-
coenzyme M isozyme MT2-A, pH 7.2, 23°C Methanosarcina barkeri
9
-
3-Mercaptopropionate isozyme MT2-A, pH 7.2, 23°C Methanosarcina barkeri
10
-
3-Mercaptopropionate isozyme MT2-M, pH 7.2, 23°C Methanosarcina barkeri

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ both isozymes are zinc-containing metalloproteins, zinc involvement in catalysis of coenzyme M methylation Methanosarcina barkeri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
HSCoM + methylcobalamin Methanosarcina barkeri
-
CH3-SCoM + cob(I)alamin + H+
-
r
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M Methanosarcina barkeri heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
-
r

Organism

Organism UniProt Comment Textmining
Methanosarcina barkeri O30640 isozymes MT2-A and MT2-M encoded by genes cmtA and cmtM
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
HSCoM + methylcobalamin
-
Methanosarcina barkeri CH3-SCoM + cob(I)alamin + H+
-
r
additional information conversions of monomethylamine and dimethylamine to CH3-SCoM are dependent upon MT2-A, and are not supported by MT2-M, both isozymes catalyze S-methylation of 2-thioethanesulfonate, i.e. coenzyme M, and exhibit similar apparent Km values for coenzyme M, isozymes substrate specificities, overview Methanosarcina barkeri ?
-
?
[methyl-Co(III) dimethylamine-specific corrinoid protein] + coenzyme M isozyme MT2-A, not MT2-M Methanosarcina barkeri methyl-CoM + [Co(I) dimethylamine-specific corrinoid protein]
-
r
[methyl-Co(III) monomethylamine-specific corrinoid protein] + coenzyme M isozyme MT2-A, not MT2-M Methanosarcina barkeri methyl-CoM + [Co(I) monomethylamine-specific corrinoid protein]
-
r
[methyl-Co(III) trimethylamine-specific corrinoid protein] + 3-mercaptopropionate 3-mercaptopropionate is a coenzyme M analogue Methanosarcina barkeri methyl-3-mercaptopropionate + [Co(I) trimethylamine-specific corrinoid protein]
-
?
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction Methanosarcina barkeri methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
-
r
[methyl-Co(III) trimethylamine-specific corrinoid protein] + coenzyme M isozymes MT2-A and MT2-M, heterolytic cleavage of the methylcobamide carbon-cobalt bond with cob(I)alamin as the major product of the reaction Methanosarcina barkeri methyl-CoM + [Co(I) trimethylamine-specific corrinoid protein]
-
r

Subunits

Subunits Comment Organism
? x * 36000-37000, recombinant isozymes MT2-A and MT2-M, SDS-PAGE Methanosarcina barkeri

Synonyms

Synonyms Comment Organism
methylcobamide:coenzyme M methyltransferase
-
Methanosarcina barkeri
MT2
-
Methanosarcina barkeri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
23
-
assay at Methanosarcina barkeri

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
additional information no enzyme-bound organic or inorganic cofactors Methanosarcina barkeri

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.005
-
pH 7.2, 23°C Methanosarcina barkeri EDTA
0.05
-
pH 7.2, 23°C Methanosarcina barkeri EGTA
0.07
-
pH 7.2, 23°C Methanosarcina barkeri 1,10-phenanthroline

General Information

General Information Comment Organism
additional information the enzyme shows an active site geometry in which coenzyme M is bound both by S-coordination to zinc, and electrostatic interaction of the sulfonate with a cationic group on the enzyme Methanosarcina barkeri