BRENDA - Enzyme Database

The role of zinc in the methylation of the coenzyme M thiol group in methanol:coenzyme M methyltransferase from Methanosarcina barkeri: new insights from X-ray absorption spectroscopy

Krüer, M.; Haumann, M.; Meyer-Klaucke, W.; Thauer, R.; Dau, H.; Eur. J. Biochem. 269, 2117-2123 (2002)

Data extracted from this reference:

Activating Compound
EC Number
Activating Compound
Commentary
Organism
Structure
2.1.1.251
additional information
ATP and/or MgCl2 do not stimulate the MMPA:CoM methyltransferase reactions mediated by the purified methylthiol: CoM methyltransferase
Methanosarcina barkeri
2.1.1.251
Ti(III) citrate
not essential activation
Methanosarcina barkeri
Cloned(Commentary)
EC Number
Commentary
Organism
2.1.1.246
gene mtaA, sequence comparison, expression of His-tagged MtaA in Escherichia coli strain M15
Methanosarcina barkeri
Engineering
EC Number
Amino acid exchange
Commentary
Organism
2.1.1.246
C239A
site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme
Methanosarcina barkeri
2.1.1.246
H237A
site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme
Methanosarcina barkeri
Metals/Ions
EC Number
Metals/Ions
Commentary
Organism
Structure
2.1.1.246
Zn2+
dependent on, wild-type MtaA has a zinc content of 0.91 mol/mol, binding structure, overview
Methanosarcina barkeri
Molecular Weight [Da]
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.1.1.251
480000
-
-
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]
-
-
r
2.1.1.246
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
Methanosarcina barkeri Fusaro, DSM 804
-
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
r
2.1.1.246
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
Methanosarcina barkeri Fusaro / DSM 804
-
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
r
2.1.1.251
dimethylsulfide + coenzyme M
Methanosarcina barkeri
-
methyl-CoM + methanethiol
-
-
?
2.1.1.251
dimethylsulfide + coenzyme M
Methanosarcina barkeri Fusaro, DSM 804
-
methyl-CoM + methanethiol
-
-
?
2.1.1.251
dimethylsulfide + coenzyme M
Methanosarcina barkeri Fusaro / DSM 804
-
methyl-CoM + methanethiol
-
-
?
2.1.1.251
methanethiol + coenzyme M
Methanosarcina barkeri
-
methyl-CoM + hydrogen sulfide
-
-
?
2.1.1.251
methylmercaptopropionate + coenzyme M
Methanosarcina barkeri
-
methyl-CoM + mercaptopropionate
-
-
r
Organism
EC Number
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
2.1.1.246
Methanosarcina barkeri
-
DSM 804, gene mtaA
-
2.1.1.246
Methanosarcina barkeri Fusaro / DSM 804
-
DSM 804, gene mtaA
-
2.1.1.251
Methanosarcina barkeri
-
-
-
2.1.1.251
Methanosarcina barkeri Fusaro, DSM 804
-
-
-
Source Tissue
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.251
additional information
methylated thiol-dependent methanogenesis in cell extract is a function of the growth substrate
Methanosarcina barkeri
-
Specific Activity [micromol/min/mg]
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.1.1.246
0.01
-
purified recombinant mutant C239A MtaA, pH 7.0, 37°C
Methanosarcina barkeri
2.1.1.246
0.02
-
purified recombinant mutant H237A MtaA, pH 7.0, 37°C
Methanosarcina barkeri
2.1.1.246
0.3
-
purified recombinant wild-type MtaA, pH 7.0, 37°C
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
-
717563
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
2.1.1.246
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
717563
Methanosarcina barkeri Fusaro, DSM 804
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
2.1.1.246
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
717563
Methanosarcina barkeri Fusaro / DSM 804
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
2.1.1.251
3-methylmercapto-1-propanol + coenzyme M
-
717563
Methanosarcina barkeri
methyl-CoM + 3-mercapto-1-propanol
-
-
-
?
2.1.1.251
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M
-
717563
Methanosarcina barkeri
methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
-
-
-
?
2.1.1.251
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M
-
717563
Methanosarcina barkeri Fusaro, DSM 804
methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
-
-
-
?
2.1.1.251
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M
-
717563
Methanosarcina barkeri Fusaro / DSM 804
methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
-
-
-
?
2.1.1.251
dimethylsulfide + coenzyme M
-
717563
Methanosarcina barkeri
methyl-CoM + methanethiol
-
-
-
?
2.1.1.251
dimethylsulfide + coenzyme M
-
717563
Methanosarcina barkeri Fusaro, DSM 804
methyl-CoM + methanethiol
-
-
-
?
2.1.1.251
dimethylsulfide + coenzyme M
-
717563
Methanosarcina barkeri Fusaro / DSM 804
methyl-CoM + methanethiol
-
-
-
?
2.1.1.251
methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein]
-
717563
Methanosarcina barkeri
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
-
-
-
?
2.1.1.251
methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein]
-
717563
Methanosarcina barkeri Fusaro, DSM 804
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
-
-
-
?
2.1.1.251
methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein]
-
717563
Methanosarcina barkeri Fusaro / DSM 804
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
-
-
-
?
2.1.1.251
methanethiol + coenzyme M
-
717563
Methanosarcina barkeri
methyl-CoM + hydrogen sulfide
-
-
-
?
2.1.1.251
methylmercaptopropionate + coenzyme M
-
717563
Methanosarcina barkeri
methyl-CoM + mercaptopropionate
-
-
-
r
2.1.1.251
additional information
the methylthiol:CoM methyltransferase reaction is initiated only with the enzyme-bound corrinoid in the methylated state. CoM can demethylate, and dimethylsulfide and methylmercaptoproionate can remethylate, the corrinoid cofactor
717563
Methanosarcina barkeri
?
-
-
-
-
2.1.1.251
additional information
the methylthiol:CoM methyltransferase reaction is initiated only with the enzyme-bound corrinoid in the methylated state. CoM can demethylate, and dimethylsulfide and methylmercaptoproionate can remethylate, the corrinoid cofactor
717563
Methanosarcina barkeri Fusaro, DSM 804
?
-
-
-
-
2.1.1.251
additional information
the methylthiol:CoM methyltransferase reaction is initiated only with the enzyme-bound corrinoid in the methylated state. CoM can demethylate, and dimethylsulfide and methylmercaptoproionate can remethylate, the corrinoid cofactor
717563
Methanosarcina barkeri Fusaro / DSM 804
?
-
-
-
-
Temperature Optimum [°C]
EC Number
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
2.1.1.246
37
-
assay at
Methanosarcina barkeri
2.1.1.251
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
2.1.1.251
7
-
assay at
Methanosarcina barkeri
Activating Compound (protein specific)
EC Number
Activating Compound
Commentary
Organism
Structure
2.1.1.251
additional information
ATP and/or MgCl2 do not stimulate the MMPA:CoM methyltransferase reactions mediated by the purified methylthiol: CoM methyltransferase
Methanosarcina barkeri
2.1.1.251
Ti(III) citrate
not essential activation
Methanosarcina barkeri
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
2.1.1.246
gene mtaA, sequence comparison, expression of His-tagged MtaA in Escherichia coli strain M15
Methanosarcina barkeri
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
Organism
2.1.1.246
C239A
site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme
Methanosarcina barkeri
2.1.1.246
H237A
site-directed mutagenesis, mutation of the residue involved in zinc coordination in MtaA results in reduced zinc content and reduced activity compared to the wild-type enzyme
Methanosarcina barkeri
Metals/Ions (protein specific)
EC Number
Metals/Ions
Commentary
Organism
Structure
2.1.1.246
Zn2+
dependent on, wild-type MtaA has a zinc content of 0.91 mol/mol, binding structure, overview
Methanosarcina barkeri
Molecular Weight [Da] (protein specific)
EC Number
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
2.1.1.251
480000
-
-
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]
-
-
r
2.1.1.246
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
Methanosarcina barkeri Fusaro, DSM 804
-
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
r
2.1.1.246
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
Methanosarcina barkeri Fusaro / DSM 804
-
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
r
2.1.1.251
dimethylsulfide + coenzyme M
Methanosarcina barkeri
-
methyl-CoM + methanethiol
-
-
?
2.1.1.251
dimethylsulfide + coenzyme M
Methanosarcina barkeri Fusaro, DSM 804
-
methyl-CoM + methanethiol
-
-
?
2.1.1.251
dimethylsulfide + coenzyme M
Methanosarcina barkeri Fusaro / DSM 804
-
methyl-CoM + methanethiol
-
-
?
2.1.1.251
methanethiol + coenzyme M
Methanosarcina barkeri
-
methyl-CoM + hydrogen sulfide
-
-
?
2.1.1.251
methylmercaptopropionate + coenzyme M
Methanosarcina barkeri
-
methyl-CoM + mercaptopropionate
-
-
r
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
2.1.1.251
additional information
methylated thiol-dependent methanogenesis in cell extract is a function of the growth substrate
Methanosarcina barkeri
-
Specific Activity [micromol/min/mg] (protein specific)
EC Number
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2.1.1.246
0.01
-
purified recombinant mutant C239A MtaA, pH 7.0, 37°C
Methanosarcina barkeri
2.1.1.246
0.02
-
purified recombinant mutant H237A MtaA, pH 7.0, 37°C
Methanosarcina barkeri
2.1.1.246
0.3
-
purified recombinant wild-type MtaA, pH 7.0, 37°C
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
-
717563
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
2.1.1.246
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
717563
Methanosarcina barkeri Fusaro, DSM 804
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
2.1.1.246
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
717563
Methanosarcina barkeri Fusaro / DSM 804
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
2.1.1.251
3-methylmercapto-1-propanol + coenzyme M
-
717563
Methanosarcina barkeri
methyl-CoM + 3-mercapto-1-propanol
-
-
-
?
2.1.1.251
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M
-
717563
Methanosarcina barkeri
methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
-
-
-
?
2.1.1.251
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M
-
717563
Methanosarcina barkeri Fusaro, DSM 804
methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
-
-
-
?
2.1.1.251
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + coenzyme M
-
717563
Methanosarcina barkeri Fusaro / DSM 804
methyl-CoM + a [Co(I) methylated-thiol-specific corrinoid protein]
-
-
-
?
2.1.1.251
dimethylsulfide + coenzyme M
-
717563
Methanosarcina barkeri
methyl-CoM + methanethiol
-
-
-
?
2.1.1.251
dimethylsulfide + coenzyme M
-
717563
Methanosarcina barkeri Fusaro, DSM 804
methyl-CoM + methanethiol
-
-
-
?
2.1.1.251
dimethylsulfide + coenzyme M
-
717563
Methanosarcina barkeri Fusaro / DSM 804
methyl-CoM + methanethiol
-
-
-
?
2.1.1.251
methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein]
-
717563
Methanosarcina barkeri
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
-
-
-
?
2.1.1.251
methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein]
-
717563
Methanosarcina barkeri Fusaro, DSM 804
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
-
-
-
?
2.1.1.251
methanethiol + a [Co(I) methylated-thiol-specific corrinoid protein]
-
717563
Methanosarcina barkeri Fusaro / DSM 804
a [methyl-Co(III) methylated-thiol-specific corrinoid protein] + hydrogen sulfide
-
-
-
?
2.1.1.251
methanethiol + coenzyme M
-
717563
Methanosarcina barkeri
methyl-CoM + hydrogen sulfide
-
-
-
?
2.1.1.251
methylmercaptopropionate + coenzyme M
-
717563
Methanosarcina barkeri
methyl-CoM + mercaptopropionate
-
-
-
r
2.1.1.251
additional information
the methylthiol:CoM methyltransferase reaction is initiated only with the enzyme-bound corrinoid in the methylated state. CoM can demethylate, and dimethylsulfide and methylmercaptoproionate can remethylate, the corrinoid cofactor
717563
Methanosarcina barkeri
?
-
-
-
-
2.1.1.251
additional information
the methylthiol:CoM methyltransferase reaction is initiated only with the enzyme-bound corrinoid in the methylated state. CoM can demethylate, and dimethylsulfide and methylmercaptoproionate can remethylate, the corrinoid cofactor
717563
Methanosarcina barkeri Fusaro, DSM 804
?
-
-
-
-
2.1.1.251
additional information
the methylthiol:CoM methyltransferase reaction is initiated only with the enzyme-bound corrinoid in the methylated state. CoM can demethylate, and dimethylsulfide and methylmercaptoproionate can remethylate, the corrinoid cofactor
717563
Methanosarcina barkeri Fusaro / DSM 804
?
-
-
-
-
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
2.1.1.251
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
2.1.1.251
7
-
assay at
Methanosarcina barkeri
General Information
EC Number
General Information
Commentary
Organism
2.1.1.251
metabolism
pathways of dimethylsulfide- and methanethiol-dependent CoM methylation are regulated. Stimulation of methanogenesis in cell extract is due to the inherent ability of the purified 480-kDa CoM methylase to function as a methylthiol:CoM methyltransferase. In the case of CoM methylation by trimethylamine, dimethylamine, monomethylamine, or methanol, separate proteins specific for each substrate exist
Methanosarcina barkeri
2.1.1.251
additional information
methylated thiol-dependent methanogenesis in cell extract is a function of the growth substrate, methanogenesis from either diethylsulfide or methylmercaptopropionate in cell extracts is coupled with the formation of methanethiol or mercaptopropionate, respectively. Consumption of methanethiol itself for methane formation also occurs. Dimethylsulfide is converted to methane by an initial demethylation which results in the formation of methanethiol. number of other compounds, including dimethylsulfoniopropionate, alanine, methionine, glycine, sarcoscine, N,N-dimethyl glycine, betaine, trimethylamine, choline, creatinine, and acetone, are not converted to methane at significant rates
Methanosarcina barkeri
2.1.1.251
physiological function
the 480-kDa corrinoid protein functions as a CoM methylase during methanogenesis from dimethylsulfide and methylmercaptopropionate, since the monomethylamine corrinoid protein and the A isozyme of methylcobamide:CoM methyltransferase, EC 2.1.1.247, do not catalyze CoM methylation with methylated thiols
Methanosarcina barkeri
General Information (protein specific)
EC Number
General Information
Commentary
Organism
2.1.1.251
metabolism
pathways of dimethylsulfide- and methanethiol-dependent CoM methylation are regulated. Stimulation of methanogenesis in cell extract is due to the inherent ability of the purified 480-kDa CoM methylase to function as a methylthiol:CoM methyltransferase. In the case of CoM methylation by trimethylamine, dimethylamine, monomethylamine, or methanol, separate proteins specific for each substrate exist
Methanosarcina barkeri
2.1.1.251
additional information
methylated thiol-dependent methanogenesis in cell extract is a function of the growth substrate, methanogenesis from either diethylsulfide or methylmercaptopropionate in cell extracts is coupled with the formation of methanethiol or mercaptopropionate, respectively. Consumption of methanethiol itself for methane formation also occurs. Dimethylsulfide is converted to methane by an initial demethylation which results in the formation of methanethiol. number of other compounds, including dimethylsulfoniopropionate, alanine, methionine, glycine, sarcoscine, N,N-dimethyl glycine, betaine, trimethylamine, choline, creatinine, and acetone, are not converted to methane at significant rates
Methanosarcina barkeri
2.1.1.251
physiological function
the 480-kDa corrinoid protein functions as a CoM methylase during methanogenesis from dimethylsulfide and methylmercaptopropionate, since the monomethylamine corrinoid protein and the A isozyme of methylcobamide:CoM methyltransferase, EC 2.1.1.247, do not catalyze CoM methylation with methylated thiols
Methanosarcina barkeri