BRENDA - Enzyme Database
show all sequences of 2.1.1.246

Methyl-coenzyme M formation in methanogenic archaea. Involvement of zinc in coenzyme M activation

Sauer, K.; Thauer, R.K.; Eur. J. Biochem. 267, 2498-2504 (2000)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
overexpression of His-tagged inactive MtaA apoprotein in Escherichia coli strain M15 grown in the presence of 2 mM EDTA
Methanosarcina barkeri
Inhibitors
Inhibitors
Commentary
Organism
Structure
EDTA
75% inhibition at 1 mM, complete inhibition at 2 mM, reversible by Zn2+ addition, competitive versus Zn2+, kinetics, overview
Methanosarcina barkeri
additional information
1 mm nitrilotriacetic acid has almost no effect on the MtaA activity
Methanosarcina barkeri
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
required, the apoprotein reacts with zinc or cobalt to the fully active holoenzyme
Methanosarcina barkeri
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
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]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
x * 50000
Methanosarcina barkeri
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
Methanosarcina barkeri
-
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanosarcina barkeri
-
gene mtaA
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged apo MtaA from Escherichia coli strain M15 by nickel affinity and anionexchange chromatography
Methanosarcina barkeri
Reaction
Reaction
Commentary
Organism
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
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2
-
purified Zn2+-containing holoenzyme, pH 7.0, 37°C
Methanosarcina barkeri
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
717562
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
?
Subunits
Subunits
Commentary
Organism
?
x * 50000
Methanosarcina barkeri
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Methanosarcina barkeri
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Methanosarcina barkeri
Cloned(Commentary) (protein specific)
Commentary
Organism
overexpression of His-tagged inactive MtaA apoprotein in Escherichia coli strain M15 grown in the presence of 2 mM EDTA
Methanosarcina barkeri
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
EDTA
75% inhibition at 1 mM, complete inhibition at 2 mM, reversible by Zn2+ addition, competitive versus Zn2+, kinetics, overview
Methanosarcina barkeri
additional information
1 mm nitrilotriacetic acid has almost no effect on the MtaA activity
Methanosarcina barkeri
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
required, the apoprotein reacts with zinc or cobalt to the fully active holoenzyme
Methanosarcina barkeri
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
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] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
50000
-
x * 50000
Methanosarcina barkeri
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
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)
Commentary
Organism
recombinant His-tagged apo MtaA from Escherichia coli strain M15 by nickel affinity and anionexchange chromatography
Methanosarcina barkeri
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
2
-
purified Zn2+-containing holoenzyme, pH 7.0, 37°C
Methanosarcina barkeri
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
717562
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 50000
Methanosarcina barkeri
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Methanosarcina barkeri
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
assay at
Methanosarcina barkeri
General Information
General Information
Commentary
Organism
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
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
General Information (protein specific)
General Information
Commentary
Organism
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
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
Other publictions for EC 2.1.1.246
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
698630
Opulencia
Physiology and posttranscripti ...
Methanosarcina acetivorans
J. Bacteriol.
191
6928-6935
2009
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1
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3
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1
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2
3
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1
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3
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1
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681980
Pritchett
Genetic, physiological and bio ...
Methanosarcina acetivorans
Mol. Microbiol.
56
1183-1194
2005
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4
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2
2
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717563
Krüer
The role of zinc in the methyl ...
Methanosarcina barkeri, Methanosarcina barkeri Fusaro / DSM 804
Eur. J. Biochem.
269
2117-2123
2002
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1
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2
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1
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3
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12
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1
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717609
Ding
Genomic and proteomic analyses ...
Methanosarcina thermophila, Methanosarcina thermophila TM-1
FEMS Microbiol. Lett.
215
127-132
2002
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11
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1
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1
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717562
Sauer
Methyl-coenzyme M formation in ...
Methanosarcina barkeri
Eur. J. Biochem.
267
2498-2504
2000
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1
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2
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3
1
1
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1
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717561
Sauer
Methanol:coenzyme M methyltran ...
Methanosarcina barkeri
Eur. J. Biochem.
261
674-681
1999
3
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1
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1
1
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1
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1
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1
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1
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2
2
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717559
Sauer
Methanol:coenzyme M methyltran ...
Methanosarcina barkeri
Eur. J. Biochem.
253
698-705
1998
1
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1
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1
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1
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4
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3
3
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485665
Sauer
Methanol:coenzyme M methyltran ...
Methanosarcina barkeri
Eur. J. Biochem.
249
280-285
1997
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1
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717557
Harms
Methylcobalamin:coenzyme M met ...
Methanosarcina barkeri, Methanosarcina barkeri DSM 804
Eur. J. Biochem.
235
653-659
1996
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1
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717753
LeClerc
Methylcobamide:coenzyme M meth ...
Methanosarcina barkeri
J. Biol. Chem.
271
18725-18731
1996
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