BRENDA - Enzyme Database
show all sequences of 2.1.1.246

Methylcobamide:coenzyme M methyltransferase isozymes from Methanosarcina barkeri. Physicochemical characterization, cloning, sequence analysis, and heterologous gene expression

LeClerc, G.M.; Grahame, D.A.; J. Biol. Chem. 271, 18725-18731 (1996)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
genes cmtA and cmtM, DNA and amino acid sequence determination and analysis, expressionin Escherichia coli strain XL-1 Blue
Methanosarcina barkeri
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics of isozymes MT2-A and MT2-M, overview
Methanosarcina barkeri
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
-
Methanosarcina barkeri
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
x * 34000, isozymes MT2-A and MT2-M, SDS-PAGE, x * 36700, about, isozyme MT2-A, sequence calculation
Methanosarcina barkeri
36700
-
x * 34000, isozymes MT2-A and MT2-M, SDS-PAGE, x * 36700, about, isozyme MT2-A, sequence calculation
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]
-
-
r
additional information
Methanosarcina barkeri
conversions of monomethylamine and dimethylamine to CH3-SCoM are dependent upon MT2-A, and are not supported by MT2-M. In contrast, MT2-M acts specifically in metabolism of methanol, but does not substitute for MT2-A in conversion of monomethylamine or dimethylamine. Nevertheless, both isozymes are capable of supporting the conversion of trimethylamine
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanosarcina barkeri
O30640
isozymes MT2-A and MT2-M encoded by genes cmtA and cmtM
-
Source Tissue
Source Tissue
Commentary
Organism
Textmining
cell culture
the isozymes MT2-A and MT2-M are differentially expressed depending upon the substrate available for growth
Methanosarcina barkeri
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.154
-
MT2 activity in recombinant Escherichia coli cells transfected with gene cmtM, pH 7.2, 37°C
Methanosarcina barkeri
1.21
-
MT2 activity in recombinant Escherichia coli cells transfected with gene cmtA, pH 7.2, 37°C
Methanosarcina barkeri
2.2
-
MT2 activity in cells grown on trimethylamine, pH 7.2, 37°C
Methanosarcina barkeri
7.5
-
MT2 activity in cells grown on methanol, pH 7.2, 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] + 3-mercaptopropanoic acid
-
717753
Methanosarcina barkeri
methyl-3-mercaptopropanoic acid + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
717753
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
the enzyme methylcobamide:CoM methyltransferase, MT2, catalyzes the transfer of the methyl group from the MT1-bound methylcobamide prosthetic group to coenzyme M
717753
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
additional information
conversions of monomethylamine and dimethylamine to CH3-SCoM are dependent upon MT2-A, and are not supported by MT2-M. In contrast, MT2-M acts specifically in metabolism of methanol, but does not substitute for MT2-A in conversion of monomethylamine or dimethylamine. Nevertheless, both isozymes are capable of supporting the conversion of trimethylamine
717753
Methanosarcina barkeri
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 34000, isozymes MT2-A and MT2-M, SDS-PAGE, x * 36700, about, isozyme MT2-A, sequence calculation
Methanosarcina barkeri
More
the isozymes MT2-A and MT2-M differ in their overall charge
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
7.2
-
assay at
Methanosarcina barkeri
Cloned(Commentary) (protein specific)
Commentary
Organism
genes cmtA and cmtM, DNA and amino acid sequence determination and analysis, expressionin Escherichia coli strain XL-1 Blue
Methanosarcina barkeri
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
steady-state kinetics of isozymes MT2-A and MT2-M, overview
Methanosarcina barkeri
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
-
Methanosarcina barkeri
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
34000
-
x * 34000, isozymes MT2-A and MT2-M, SDS-PAGE, x * 36700, about, isozyme MT2-A, sequence calculation
Methanosarcina barkeri
36700
-
x * 34000, isozymes MT2-A and MT2-M, SDS-PAGE, x * 36700, about, isozyme MT2-A, sequence calculation
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]
-
-
r
additional information
Methanosarcina barkeri
conversions of monomethylamine and dimethylamine to CH3-SCoM are dependent upon MT2-A, and are not supported by MT2-M. In contrast, MT2-M acts specifically in metabolism of methanol, but does not substitute for MT2-A in conversion of monomethylamine or dimethylamine. Nevertheless, both isozymes are capable of supporting the conversion of trimethylamine
?
-
-
-
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
cell culture
the isozymes MT2-A and MT2-M are differentially expressed depending upon the substrate available for growth
Methanosarcina barkeri
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.154
-
MT2 activity in recombinant Escherichia coli cells transfected with gene cmtM, pH 7.2, 37°C
Methanosarcina barkeri
1.21
-
MT2 activity in recombinant Escherichia coli cells transfected with gene cmtA, pH 7.2, 37°C
Methanosarcina barkeri
2.2
-
MT2 activity in cells grown on trimethylamine, pH 7.2, 37°C
Methanosarcina barkeri
7.5
-
MT2 activity in cells grown on methanol, pH 7.2, 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] + 3-mercaptopropanoic acid
-
717753
Methanosarcina barkeri
methyl-3-mercaptopropanoic acid + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
717753
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
the enzyme methylcobamide:CoM methyltransferase, MT2, catalyzes the transfer of the methyl group from the MT1-bound methylcobamide prosthetic group to coenzyme M
717753
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
additional information
conversions of monomethylamine and dimethylamine to CH3-SCoM are dependent upon MT2-A, and are not supported by MT2-M. In contrast, MT2-M acts specifically in metabolism of methanol, but does not substitute for MT2-A in conversion of monomethylamine or dimethylamine. Nevertheless, both isozymes are capable of supporting the conversion of trimethylamine
717753
Methanosarcina barkeri
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 34000, isozymes MT2-A and MT2-M, SDS-PAGE, x * 36700, about, isozyme MT2-A, sequence calculation
Methanosarcina barkeri
More
the isozymes MT2-A and MT2-M differ in their overall charge
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
7.2
-
assay at
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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1
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1
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1
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2
3
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1
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1
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1
1
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681980
Pritchett
Genetic, physiological and bio ...
Methanosarcina acetivorans
Mol. Microbiol.
56
1183-1194
2005
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1
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4
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1
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1
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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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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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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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1
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1
1
1
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1
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2
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1
1
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1
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1
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1
1
1
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1
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2
2
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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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2
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1
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2
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1
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2
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2
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1
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1
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3
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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
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2
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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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1
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1
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1
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1
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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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