BRENDA - Enzyme Database
show all sequences of 2.1.1.246

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
Activating Compound
Commentary
Organism
Structure
Ti(III) citrate
-
Methanosarcina barkeri
Cloned(Commentary)
Commentary
Organism
genes mtaA and mtaB, expression of N-terminally His-tagged isozymes MtaA and MtbA in Escherichia coli strain M15
Methanosarcina barkeri
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
required
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
-
-
-
Purification (Commentary)
Commentary
Organism
recombinant N-terminally His-tagged isozymes MtaA and MtbA from Escherichia coli strain M15 by nickel affinity chromatography
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
-
717559
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
?
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]
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
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Ti(III) citrate
-
Methanosarcina barkeri
Cloned(Commentary) (protein specific)
Commentary
Organism
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)
Metals/Ions
Commentary
Organism
Structure
Zn2+
required
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 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)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
a [methyl-Co(III) methanol-specific corrinoid protein] + coenzyme M
-
717559
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
?
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)
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
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
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
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)
General Information
Commentary
Organism
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
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
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
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
-
-
1
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-
-
-
-
-
-
-
-
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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
-
4
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1
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1
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1
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-
-
-
-
-
-
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2
2
-
-
-
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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3
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3
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1
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1
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1
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3
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3
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1
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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
-
-
-
2
-
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3
1
1
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1
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1
1
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1
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1
1
1
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1
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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
2
-
-
-
717561
Sauer
Methanol:coenzyme M methyltran ...
Methanosarcina barkeri
Eur. J. Biochem.
261
674-681
1999
3
-
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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2
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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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-
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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
-
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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2
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1
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1
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1
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2
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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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1
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3
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1
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1
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1
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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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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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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1
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-
717753
LeClerc
Methylcobamide:coenzyme M meth ...
Methanosarcina barkeri
J. Biol. Chem.
271
18725-18731
1996
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1
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1
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1
2
2
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3
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1
4
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4
2
1
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1
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1
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1
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1
2
2
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1
4
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4
2
1
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1
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