BRENDA - Enzyme Database
show all sequences of 2.1.1.246

Methanol:coenzyme M methyltransferase from Methanosarcina barkeri - substitution of the corrinoid harbouring subunit MtaC by free cob(I)alamin

Sauer, K.; Thauer, R.K.; Eur. J. Biochem. 261, 674-681 (1999)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
methanol
MtaB plus methanol positively affect the catalytic efficiency of MtaA. activation of MtaA by MtaB is methanol-dependent. Methylation of cob(I)inamide with methanol is dependent on imidazole but not on the demethylation of methylcob(III)inamide with coenzyme M. The demethylation reaction is even inhibited by imidazole
Methanosarcina barkeri
MtaB
MtaB plus methanol positively affect the catalytic efficiency of MtaA. activation of MtaA by MtaB is methanol-dependent. Methylation of cob(I)inamide with methanol is dependent on imidazole but not on the demethylation of methylcob(III)inamide with coenzyme M. The demethylation reaction is even inhibited by imidazole
Methanosarcina barkeri
Ti(III) citrate
increases the specific activity of MtaA by 60% and decreases the apparent Km for methylcob(III)-alamin from 0.003 mM to below 0.001 mM
Methanosarcina barkeri
Cloned(Commentary)
Commentary
Organism
gene mtaA, expression of His-tagged MtaA in Escherichia coli strain M15
Methanosarcina barkeri
Inhibitors
Inhibitors
Commentary
Organism
Structure
imidazole
the demethylation of cob(I)inamide reaction is inhibited by imidazole. Imidazole does not inhibit methyltransfer from methylcob(III)alamin to coenzyme M at 10 mM
Methanosarcina barkeri
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
MtaA kinetics, overview. Demethylation of methylcob(III)alamin catalysed by MtaA alone exhibit apparent Km for cob(I)alamin and methylcob(III)alamin of above 1 mm
Methanosarcina barkeri
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Co2+
Zn2+ can be substituted by Co2+
Methanosarcina barkeri
Zn2+
Mta contains 1 mol Zn2+ per mol of enzyme, Zn2+ can be substituted by Co2+
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
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanosarcina barkeri
-
gene mtaA
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged MtaA from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography to homogeneity
Methanosarcina barkeri
Specific Activity [micromol/min/mg]
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.2
-
MtaA with substrate methylcob(III)-alamin, pH 7.0, 37C
Methanosarcina barkeri
8
-
MtaA with substrate methylcob(III)inamide, 50 mM methylcob(III)inamide as substrate show an activity of 8 U/mg, approximately 40fold higher than with 50 mM methylcob(III)-alamin, pH 7.0, 37C
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
-
717561
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
additional information
in the assay for methanol:coenzyme M methyltransferase activity cob(I)alamin can be substituted by cob(I)inamide which is devoid of the nucleotide loopmethylation of cob(I)inamide with methanol is dependent on imidazole but not on the demethylation of methylcob(III)inamide with coenzyme M
717561
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
methanol
MtaB plus methanol positively affect the catalytic efficiency of MtaA. activation of MtaA by MtaB is methanol-dependent. Methylation of cob(I)inamide with methanol is dependent on imidazole but not on the demethylation of methylcob(III)inamide with coenzyme M. The demethylation reaction is even inhibited by imidazole
Methanosarcina barkeri
MtaB
MtaB plus methanol positively affect the catalytic efficiency of MtaA. activation of MtaA by MtaB is methanol-dependent. Methylation of cob(I)inamide with methanol is dependent on imidazole but not on the demethylation of methylcob(III)inamide with coenzyme M. The demethylation reaction is even inhibited by imidazole
Methanosarcina barkeri
Ti(III) citrate
increases the specific activity of MtaA by 60% and decreases the apparent Km for methylcob(III)-alamin from 0.003 mM to below 0.001 mM
Methanosarcina barkeri
Cloned(Commentary) (protein specific)
Commentary
Organism
gene mtaA, expression of His-tagged MtaA in Escherichia coli strain M15
Methanosarcina barkeri
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
imidazole
the demethylation of cob(I)inamide reaction is inhibited by imidazole. Imidazole does not inhibit methyltransfer from methylcob(III)alamin to coenzyme M at 10 mM
Methanosarcina barkeri
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
MtaA kinetics, overview. Demethylation of methylcob(III)alamin catalysed by MtaA alone exhibit apparent Km for cob(I)alamin and methylcob(III)alamin of above 1 mm
Methanosarcina barkeri
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Co2+
Zn2+ can be substituted by Co2+
Methanosarcina barkeri
Zn2+
Mta contains 1 mol Zn2+ per mol of enzyme, Zn2+ can be substituted by Co2+
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
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged MtaA from Escherichia coli strain M15 by nickel affinity and anion exchange chromatography to homogeneity
Methanosarcina barkeri
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [mol/min/mg]
Specific Activity Maximum [mol/min/mg]
Commentary
Organism
0.2
-
MtaA with substrate methylcob(III)-alamin, pH 7.0, 37C
Methanosarcina barkeri
8
-
MtaA with substrate methylcob(III)inamide, 50 mM methylcob(III)inamide as substrate show an activity of 8 U/mg, approximately 40fold higher than with 50 mM methylcob(III)-alamin, pH 7.0, 37C
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
-
717561
Methanosarcina barkeri
methyl-CoM + a [Co(I) methanol-specific corrinoid protein]
-
-
-
r
additional information
in the assay for methanol:coenzyme M methyltransferase activity cob(I)alamin can be substituted by cob(I)inamide which is devoid of the nucleotide loopmethylation of cob(I)inamide with methanol is dependent on imidazole but not on the demethylation of methylcob(III)inamide with coenzyme M
717561
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
metabolism
methyl-coenzyme M formation from coenzyme M and methanol in Methanosarcina barkeri is catalysed by an enzyme system composed of three polypeptides MtaA, MtaB and MtaC, the latter of which harbours a corrinoid prosthetic group. We report here that MtaC can be substituted by free cob(I)alamin which is methylated with methanol in an MtaB-catalysed reaction and demethylated with coenzyme M in an MtaA-catalysed reaction
Methanosarcina barkeri
physiological function
a positive effect of MtaA on the catalytic efficiency of MtaB is specific for MtaA. In the absence of MtaA no effect is observed, while in the presence of MtaA the formation of methylcob(III)alamin from methanol and cob(I)alamin is apparently inhibited by coenzyme M, probably because under these conditions MtaA actively catalyses the demethylation of methylcob(III)alamin. MtaB plus methanol positively affect the catalytic efficiency of MtaA
Methanosarcina barkeri
General Information (protein specific)
General Information
Commentary
Organism
metabolism
methyl-coenzyme M formation from coenzyme M and methanol in Methanosarcina barkeri is catalysed by an enzyme system composed of three polypeptides MtaA, MtaB and MtaC, the latter of which harbours a corrinoid prosthetic group. We report here that MtaC can be substituted by free cob(I)alamin which is methylated with methanol in an MtaB-catalysed reaction and demethylated with coenzyme M in an MtaA-catalysed reaction
Methanosarcina barkeri
physiological function
a positive effect of MtaA on the catalytic efficiency of MtaB is specific for MtaA. In the absence of MtaA no effect is observed, while in the presence of MtaA the formation of methylcob(III)alamin from methanol and cob(I)alamin is apparently inhibited by coenzyme M, probably because under these conditions MtaA actively catalyses the demethylation of methylcob(III)alamin. MtaB plus methanol positively affect the catalytic efficiency of MtaA
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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681980
Pritchett
Genetic, physiological and bio ...
Methanosarcina acetivorans
Mol. Microbiol.
56
1183-1194
2005
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717563
Krer
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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717609
Ding
Genomic and proteomic analyses ...
Methanosarcina thermophila, Methanosarcina thermophila TM-1
FEMS Microbiol. Lett.
215
127-132
2002
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717562
Sauer
Methyl-coenzyme M formation in ...
Methanosarcina barkeri
Eur. J. Biochem.
267
2498-2504
2000
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717561
Sauer
Methanol:coenzyme M methyltran ...
Methanosarcina barkeri
Eur. J. Biochem.
261
674-681
1999
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717559
Sauer
Methanol:coenzyme M methyltran ...
Methanosarcina barkeri
Eur. J. Biochem.
253
698-705
1998
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485665
Sauer
Methanol:coenzyme M methyltran ...
Methanosarcina barkeri
Eur. J. Biochem.
249
280-285
1997
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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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717753
LeClerc
Methylcobamide:coenzyme M meth ...
Methanosarcina barkeri
J. Biol. Chem.
271
18725-18731
1996
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