BRENDA - Enzyme Database

Methanol:coenzyme M methyltransferase from Methanosarcina barkeri - identification of the active-site histidine in the corrinoid-harboring subunit MtaC by site-directed mutagenesis

Sauer, K.; Thauer, R.K.; Eur. J. Biochem. 253, 698-705 (1998)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
2.1.1.246
Ti(III) citrate
-
Methanosarcina barkeri
Cloned(Commentary)
EC Number
Commentary
Organism
2.1.1.246
genes mtaA and mtaB, expression of N-terminally His-tagged isozymes MtaA and MtbA in Escherichia coli strain M15
Methanosarcina barkeri
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
2.1.1.246
Zn2+
required
Methanosarcina barkeri
Natural Substrates/ Products (Substrates)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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
Primary Accession No. (UniProt)
Commentary
Textmining
2.1.1.246
Methanosarcina barkeri
-
-
-
Purification (Commentary)
EC Number
Commentary
Organism
2.1.1.246
recombinant N-terminally His-tagged isozymes MtaA and MtbA from Escherichia coli strain M15 by nickel affinity chromatography
Methanosarcina barkeri
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.1.1.246
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
717559
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
?
2.1.1.246
additional information
recombinant MtaA catalyzes the formation of methyl-coenzyme M from free CH3-cob(III)alamin and coenzyme M at specific rates comparable to those predicted for MtaA-catalyzed MtaC demethylation
717559
Methanosarcina barkeri
?
-
-
-
-
Temperature Optimum [C]
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
2.1.1.246
37
-
assay at
Methanosarcina barkeri
pH Optimum
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.1.1.246
7
-
assay at
Methanosarcina barkeri
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
2.1.1.246
Ti(III) citrate
-
Methanosarcina barkeri
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
2.1.1.246
genes mtaA and mtaB, expression of N-terminally His-tagged isozymes MtaA and MtbA in Escherichia coli strain M15
Methanosarcina barkeri
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
2.1.1.246
Zn2+
required
Methanosarcina barkeri
Natural Substrates/ Products (Substrates) (protein specific)
EC Number
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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]
-
-
?
Purification (Commentary) (protein specific)
EC Number
Commentary
Organism
2.1.1.246
recombinant N-terminally His-tagged isozymes MtaA and MtbA from Escherichia coli strain M15 by nickel affinity chromatography
Methanosarcina barkeri
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2.1.1.246
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
717559
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
?
2.1.1.246
additional information
recombinant MtaA catalyzes the formation of methyl-coenzyme M from free CH3-cob(III)alamin and coenzyme M at specific rates comparable to those predicted for MtaA-catalyzed MtaC demethylation
717559
Methanosarcina barkeri
?
-
-
-
-
Temperature Optimum [C] (protein specific)
EC Number
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
2.1.1.246
37
-
assay at
Methanosarcina barkeri
pH Optimum (protein specific)
EC Number
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
2.1.1.246
7
-
assay at
Methanosarcina barkeri
General Information
EC Number
General Information
Commentary
Organism
2.1.1.246
evolution
Methanosarcina barkeri contains an isoenzyme of MtaA designated MtbA. The isoenzyme reacts with MtaC with only 2.5% of the activity of MtaA
Methanosarcina barkeri
2.1.1.246
metabolism
the enzyme system catalyzing the formation of methyl-coenzyme M from methanol and coenzyme M in Methanosarcina barkeri is composed of the three different polypeptides MtaA, MtaB and MtaC of which MtaC harbors a corrinoid prosthetic group
Methanosarcina barkeri
2.1.1.246
additional information
the enzyme system catalyzing the formation of methyl-coenzyme M from methanol and coenzyme M in Methanosarcina barkeri is composed of the three different polypeptides MtaA, MtaB and MtaC of which MtaC harbors a corrinoid prosthetic group
Methanosarcina barkeri
General Information (protein specific)
EC Number
General Information
Commentary
Organism
2.1.1.246
evolution
Methanosarcina barkeri contains an isoenzyme of MtaA designated MtbA. The isoenzyme reacts with MtaC with only 2.5% of the activity of MtaA
Methanosarcina barkeri
2.1.1.246
metabolism
the enzyme system catalyzing the formation of methyl-coenzyme M from methanol and coenzyme M in Methanosarcina barkeri is composed of the three different polypeptides MtaA, MtaB and MtaC of which MtaC harbors a corrinoid prosthetic group
Methanosarcina barkeri
2.1.1.246
additional information
the enzyme system catalyzing the formation of methyl-coenzyme M from methanol and coenzyme M in Methanosarcina barkeri is composed of the three different polypeptides MtaA, MtaB and MtaC of which MtaC harbors a corrinoid prosthetic group
Methanosarcina barkeri