BRENDA - Enzyme Database show
show all sequences of 2.1.1.163

An Escherichia coli mutant containing only demethylmenaquinone, but not menaquinone: effects on fumarate, dimethylsulfoxide, trimethylamine N-oxide and nitrate respiration

Wissenbach, U.; Ternes, D.; Unden, G.; Arch. Microbiol. 158, 68-73 (1992)

Data extracted from this reference:

Engineering
Amino acid exchange
Commentary
Organism
additional information
mutant ubiE lacks ubiquinone due to defect in a specific methylation step of ubiquinone synthesis. Synthesis of menaquinone from demethylmenaquinone depends on the same gene ubiE. Mutant contains only demethylmenaquinone, but not menaquinone. Strain is able to grow with fumarate, trimethylamine N-oxide and dimethylsulfoxide, but not with nitrate as electron acceptor. Anaerobic respiration with fumarate and trimethylamine are catalyzed at 69% and 74% of wild-type rates, respectively. Dimethylsulfoxide respiration is reduced to 38% of wild-type, and nitrate respiration is below 8%
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-octaprenyl-1,4-naphthoquinone + S-adenosyl-L-methionine
Escherichia coli
-
2-octaprenyl-3-methyl-1,4-naphthoquinone + S-adenosyl-L-homocysteine
i.e. menaquinone
-
?
2-octaprenyl-1,4-naphthoquinone + S-adenosyl-L-methionine
Escherichia coli AN387
-
2-octaprenyl-3-methyl-1,4-naphthoquinone + S-adenosyl-L-homocysteine
i.e. menaquinone
-
?
2-octaprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine
Escherichia coli
-
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine
-
-
?
2-octaprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine
Escherichia coli AN387
-
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
-
; gene ubiE
-
Escherichia coli AN387
-
gene ubiE
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-octaprenyl-1,4-naphthoquinone + S-adenosyl-L-methionine
-
695910
Escherichia coli
2-octaprenyl-3-methyl-1,4-naphthoquinone + S-adenosyl-L-homocysteine
i.e. menaquinone
-
-
?
2-octaprenyl-1,4-naphthoquinone + S-adenosyl-L-methionine
-
695910
Escherichia coli AN387
2-octaprenyl-3-methyl-1,4-naphthoquinone + S-adenosyl-L-homocysteine
i.e. menaquinone
-
-
?
2-octaprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine
-
695910
Escherichia coli
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine
-
-
-
?
2-octaprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine
-
695910
Escherichia coli AN387
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine
-
-
-
?
Cofactor
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
S-adenosyl-L-methionine
-
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
mutant ubiE lacks ubiquinone due to defect in a specific methylation step of ubiquinone synthesis. Synthesis of menaquinone from demethylmenaquinone depends on the same gene ubiE. Mutant contains only demethylmenaquinone, but not menaquinone. Strain is able to grow with fumarate, trimethylamine N-oxide and dimethylsulfoxide, but not with nitrate as electron acceptor. Anaerobic respiration with fumarate and trimethylamine are catalyzed at 69% and 74% of wild-type rates, respectively. Dimethylsulfoxide respiration is reduced to 38% of wild-type, and nitrate respiration is below 8%
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
2-octaprenyl-1,4-naphthoquinone + S-adenosyl-L-methionine
Escherichia coli
-
2-octaprenyl-3-methyl-1,4-naphthoquinone + S-adenosyl-L-homocysteine
i.e. menaquinone
-
?
2-octaprenyl-1,4-naphthoquinone + S-adenosyl-L-methionine
Escherichia coli AN387
-
2-octaprenyl-3-methyl-1,4-naphthoquinone + S-adenosyl-L-homocysteine
i.e. menaquinone
-
?
2-octaprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine
Escherichia coli
-
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine
-
-
?
2-octaprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine
Escherichia coli AN387
-
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
2-octaprenyl-1,4-naphthoquinone + S-adenosyl-L-methionine
-
695910
Escherichia coli
2-octaprenyl-3-methyl-1,4-naphthoquinone + S-adenosyl-L-homocysteine
i.e. menaquinone
-
-
?
2-octaprenyl-1,4-naphthoquinone + S-adenosyl-L-methionine
-
695910
Escherichia coli AN387
2-octaprenyl-3-methyl-1,4-naphthoquinone + S-adenosyl-L-homocysteine
i.e. menaquinone
-
-
?
2-octaprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine
-
695910
Escherichia coli
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine
-
-
-
?
2-octaprenyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-methionine
-
695910
Escherichia coli AN387
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinone + S-adenosyl-L-homocysteine
-
-
-
?
General Information
General Information
Commentary
Organism
malfunction
in the uniE-lacking mutant strain AN70, a lack of ubiquinone occurs due to the missing methylation reaction. The mutant also contains only demethylmenaquinone, no menaquinone. Mutant respiration of DMSO is increased, while the respiration of fumarate is reduced compared to the wild-type enzyme
Escherichia coli
metabolism
the enzyme catalyzes a step in the menaquinone pathway as well as the methylation step in ubiquinone pathway, overview. Menaquinne activates the respiration of fumarate, trimethylamine N-oxide, nitrate, and DMSO
Escherichia coli
physiological function
mutant ubiE lacks ubiquinone due to defect in a specific methylation step of ubiquinone synthesis. Synthesis of menaquinone from demethylmenaquinone depends on the same gene ubiE. Mutant contains only demethylmenaquinone, but not menaquinone. Strain is able to grow with fumarate, trimethylamine N-oxide and dimethylsulfoxide, but not with nitrate as electron acceptor. Anaerobic respiration with fumarate and trimethylamine are catalyzed at 69% and 74% of wild-type rates, respectively. Dimethylsulfoxide respiration is reduced to 38% of wild-type, and nitrate respiration is below 8%
Escherichia coli
General Information (protein specific)
General Information
Commentary
Organism
malfunction
in the uniE-lacking mutant strain AN70, a lack of ubiquinone occurs due to the missing methylation reaction. The mutant also contains only demethylmenaquinone, no menaquinone. Mutant respiration of DMSO is increased, while the respiration of fumarate is reduced compared to the wild-type enzyme
Escherichia coli
metabolism
the enzyme catalyzes a step in the menaquinone pathway as well as the methylation step in ubiquinone pathway, overview. Menaquinne activates the respiration of fumarate, trimethylamine N-oxide, nitrate, and DMSO
Escherichia coli
physiological function
mutant ubiE lacks ubiquinone due to defect in a specific methylation step of ubiquinone synthesis. Synthesis of menaquinone from demethylmenaquinone depends on the same gene ubiE. Mutant contains only demethylmenaquinone, but not menaquinone. Strain is able to grow with fumarate, trimethylamine N-oxide and dimethylsulfoxide, but not with nitrate as electron acceptor. Anaerobic respiration with fumarate and trimethylamine are catalyzed at 69% and 74% of wild-type rates, respectively. Dimethylsulfoxide respiration is reduced to 38% of wild-type, and nitrate respiration is below 8%
Escherichia coli
Other publictions for EC 2.1.1.163
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)
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1
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7
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2
2
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166
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1
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1
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695912
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403-411
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1
1
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698549
Lee
A C-methyltransferase involved ...
Escherichia coli
J. Bacteriol.
179
1748-1754
1997
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2
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1
1
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698706
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Identification of a novel gene ...
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J. Biol. Chem.
272
12380-12383
1997
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1
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1
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1
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5
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1
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1
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An Escherichia coli mutant con ...
Escherichia coli, Escherichia coli AN387
Arch. Microbiol.
158
68-73
1992
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1
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4
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2
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4
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1
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1
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1
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4
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4
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3
3
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