BRENDA - Enzyme Database show
show all sequences of 2.1.1.90

Activation mechanism of methanol:5-hydroxybenzimidazolylcobamide methyltransferase from Methanosarcina barkeri

Daas, P.J.; Hagen, W.R.; Keltjens, J.T.; van der Drift, C.; Vogels, G.D.; J. Biol. Chem. 271, 22346-2251 (1996)

Data extracted from this reference:

Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Cobalt
the enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP
Methanosarcina barkeri
Iron
presence of 1.7 mol of non-heme iron per mol of enzyme
Methanosarcina barkeri
Mg2+
plays a role in binding of the corrinoid prosthetic group and in subunit association
Methanosarcina barkeri
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
121000
-
gradient PAGE, gel filtration
Methanosarcina barkeri
122000
-
gel filtration
Methanosarcina barkeri
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
methanol + a [Co(I) methanol-specific corrinoid protein]
Methanosarcina barkeri
first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
Methanosarcina barkeri DSM 800
first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Methanosarcina barkeri
-
-
-
Methanosarcina barkeri DSM 800
-
-
-
Purification (Commentary)
Commentary
Organism
-
Methanosarcina barkeri
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
methanol + a [Co(I) methanol-specific corrinoid protein]
-
727819
Methanosarcina barkeri
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme
727819
Methanosarcina barkeri
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
-
727819
Methanosarcina barkeri DSM 800
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme
727819
Methanosarcina barkeri DSM 800
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
?
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
corrinoid
the enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme
Methanosarcina barkeri
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Methanosarcina barkeri
isoelectric focusing
-
4.5
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
corrinoid
the enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme
Methanosarcina barkeri
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Cobalt
the enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP
Methanosarcina barkeri
Iron
presence of 1.7 mol of non-heme iron per mol of enzyme
Methanosarcina barkeri
Mg2+
plays a role in binding of the corrinoid prosthetic group and in subunit association
Methanosarcina barkeri
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
121000
-
gradient PAGE, gel filtration
Methanosarcina barkeri
122000
-
gel filtration
Methanosarcina barkeri
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
methanol + a [Co(I) methanol-specific corrinoid protein]
Methanosarcina barkeri
first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
Methanosarcina barkeri DSM 800
first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
-
Methanosarcina barkeri
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
methanol + a [Co(I) methanol-specific corrinoid protein]
-
727819
Methanosarcina barkeri
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme
727819
Methanosarcina barkeri
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
-
727819
Methanosarcina barkeri DSM 800
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
?
methanol + a [Co(I) methanol-specific corrinoid protein]
first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in. The enzyme only binds the methyl group of methanol when the cobalt atom of its corrinoid prosthetic groups is present in the highly reduced Co(I) state. Formation of this redox state requires H2, hydrogenase, methyltransferase activation protein, and ATP. Purified enzyme contains 1.7 corrinoids per enzyme with cobalt in the fully oxidized Co(III) state. Water and N-3 of the 5-hydroxybenzimidazolyl base serve as the upper and lower ligands, respectively. Reduction to the Co(II) level is accomplished by H2 and hydrogenase. The cob(II)amide of the enzyme has the base coordinated at this stage. Subsequent addition of methyltransferase activation protein and ATP results in the formation of base-uncoordinated Co(II) enzyme
727819
Methanosarcina barkeri DSM 800
a [methyl-Co(III) methanol-specific corrinoid protein] + H2O
-
-
-
?
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
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Methanosarcina barkeri
isoelectric focusing
-
4.5
General Information
General Information
Commentary
Organism
physiological function
first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in Methanosarcina barkeri
Methanosarcina barkeri
General Information (protein specific)
General Information
Commentary
Organism
physiological function
first of two enzymes involved in the transmethylation reaction from methanol to 2-mercaptoethanesulfonic acid in Methanosarcina barkeri
Methanosarcina barkeri
Other publictions for EC 2.1.1.90
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)
726582
Hoeppner
Structure of the corrinoid:coe ...
Methanosarcina mazei
Acta Crystallogr. Sect. D
68
1549-1557
2012
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698630
Opulencia
Physiology and posttranscripti ...
Methanosarcina acetivorans
J. Bacteriol.
191
6928-6935
2009
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680470
Bose
Differential regulation of the ...
Methanosarcina acetivorans
J. Bacteriol.
188
7274-7283
2006
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682524
Hagemeier
Insight into the mechanism of ...
Methanosarcina barkeri
Proc. Natl. Acad. Sci. USA
103
18917-18922
2006
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681980
Pritchett
Genetic, physiological and bio ...
Methanosarcina acetivorans
Mol. Microbiol.
56
1183-1194
2005
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485665
Sauer
Methanol:coenzyme M methyltran ...
Methanosarcina barkeri
Eur. J. Biochem.
249
280-285
1997
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485666
Sauer
Methanol:coenzyme M methyltran ...
Methanosarcina barkeri
Eur. J. Biochem.
243
670-677
1997
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727819
Daas
Activation mechanism of methan ...
Methanosarcina barkeri, Methanosarcina barkeri DSM 800
J. Biol. Chem.
271
22346-2251
1996
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485660
Van der Meijden
Purification and properties of ...
Methanosarcina barkeri
J. Bacteriol.
160
629-635
1984
2
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485661
Van der Meijden
Reductive activation of methan ...
Methanosarcina barkeri
Biochem. Biophys. Res. Commun.
118
760-766
1984
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485663
Van der Meijden
-
Methanol conversion in Eubacte ...
Eubacterium limosum, Methanothermobacter thermautotrophicus
Arch. Microbiol.
138
360-364
1984
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485662
Van der Meijden
Methyltransferases involved in ...
Methanosarcina barkeri
Arch. Microbiol.
134
238-242
1983
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485664
Taylor
A simplified assay for coenzym ...
Methanobacterium bryantii
J. Biol. Chem.
249
4886-4890
1974
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