BRENDA - Enzyme Database show
show all sequences of 2.1.1.253

Tetramethylammonium:coenzyme M methyltransferase system from Methanococcoides sp.

Asakawa, S.; Sauer, K.; Liesack, W.; Thauer, R.; Arch. Microbiol. 170, 220-226 (1998)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
Ti(III) citrate
dependent on
Methanosarcina barkeri
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Methanosarcina barkeri
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
x * 40000, SDS-PAGE
Methanosarcina barkeri
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanosarcina barkeri
-
gene mtqA
-
Methanosarcina barkeri NaT1
-
gene mtqA
-
Purification (Commentary)
Commentary
Organism
native enzyme by ultracentrifugation, a first step of anion exchange chromatography, hydroxyapatite chromatography, a second step of anion exchange chromatography, adsorption and again a third step of anion exchange chromatography
Methanosarcina barkeri
Source Tissue
Source Tissue
Commentary
Organism
Textmining
culture condition:tetramethylammonium-grown cell
-
Methanosarcina barkeri
-
additional information
cell extracts of strain NaT1 grown on trimethylamine rather than on tetramethylammonium are devoid of tetramethylammonium:coenzyme M methyltransferase activity
Methanosarcina barkeri
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme exhibits MT2 activity, the MT2 activity is measured by following the coenzyme-M-dependent demethylation of methylcobalamin. Tetramethylammonium:coenzyme M methyltransferase activity detected by coenzyme M methylation
717162
Methanosarcina barkeri
?
-
-
-
-
additional information
the enzyme exhibits MT2 activity, the MT2 activity is measured by following the coenzyme-M-dependent demethylation of methylcobalamin. Tetramethylammonium:coenzyme M methyltransferase activity detected by coenzyme M methylation
717162
Methanosarcina barkeri NaT1
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
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
Cofactor
Cofactor
Commentary
Organism
Structure
ATP
dependent on
Methanosarcina barkeri
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
Ti(III) citrate
dependent on
Methanosarcina barkeri
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
ATP
dependent on
Methanosarcina barkeri
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
-
Methanosarcina barkeri
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
40000
-
x * 40000, SDS-PAGE
Methanosarcina barkeri
Purification (Commentary) (protein specific)
Commentary
Organism
native enzyme by ultracentrifugation, a first step of anion exchange chromatography, hydroxyapatite chromatography, a second step of anion exchange chromatography, adsorption and again a third step of anion exchange chromatography
Methanosarcina barkeri
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
culture condition:tetramethylammonium-grown cell
-
Methanosarcina barkeri
-
additional information
cell extracts of strain NaT1 grown on trimethylamine rather than on tetramethylammonium are devoid of tetramethylammonium:coenzyme M methyltransferase activity
Methanosarcina barkeri
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme exhibits MT2 activity, the MT2 activity is measured by following the coenzyme-M-dependent demethylation of methylcobalamin. Tetramethylammonium:coenzyme M methyltransferase activity detected by coenzyme M methylation
717162
Methanosarcina barkeri
?
-
-
-
-
additional information
the enzyme exhibits MT2 activity, the MT2 activity is measured by following the coenzyme-M-dependent demethylation of methylcobalamin. Tetramethylammonium:coenzyme M methyltransferase activity detected by coenzyme M methylation
717162
Methanosarcina barkeri NaT1
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 40000, SDS-PAGE
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
cell extracts of strain NaT1 catalyze the formation of methyl-coenzyme M from coenzyme M and tetramethylammonium, EC 2.1.1.253, or trimethylamine, EC 2.1.1.250, but not from coenzyme M and dimethylamine, EC 2.1.1.249, monomethylamine, EC 2.1.1.248, or methanol, EC 2.1.1.246
Methanosarcina barkeri
General Information (protein specific)
General Information
Commentary
Organism
additional information
cell extracts of strain NaT1 catalyze the formation of methyl-coenzyme M from coenzyme M and tetramethylammonium, EC 2.1.1.253, or trimethylamine, EC 2.1.1.250, but not from coenzyme M and dimethylamine, EC 2.1.1.249, monomethylamine, EC 2.1.1.248, or methanol, EC 2.1.1.246
Methanosarcina barkeri
Other publictions for EC 2.1.1.253
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)
717162
Asakawa
Tetramethylammonium:coenzyme M ...
Methanosarcina barkeri, Methanosarcina barkeri NaT1
Arch. Microbiol.
170
220-226
1998
1
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7
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2
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1
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1
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1
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1
1
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1
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2
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2
1
1
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1
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1
1
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