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EC Tree
IUBMB Comments A flavoprotein. The enzyme catalyses a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone . The animal, but not the plant, form of the enzyme is inhibited by dicoumarol.
The taxonomic range for the selected organisms is: Escherichia coli The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
dt-diaphorase, diaphorase, quinone reductase, azoreductase, nad(p)h:quinone oxidoreductase 1, nad(p)h:quinone oxidoreductase, nad(p)h dehydrogenase, nad(p)h quinone oxidoreductase 1, ndh complex, nad(p)h quinone oxidoreductase,
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NADPH:quinone oxidoreductase
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dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone)
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flavoprotein NAD(P)H-quinone reductase
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Menadione oxidoreductase
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Menadione reductase
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NAD(P)H dehydrogenase
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NAD(P)H menadione reductase
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NAD(P)H-quinone dehydrogenase
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NAD(P)H-quinone oxidoreductase
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NAD(P)H: (quinone-acceptor)oxidoreductase
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NAD(P)H: menadione oxidoreductase
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NADH-menadione reductase
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Naphthoquinone reductase
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p-Benzoquinone reductase
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Phylloquinone reductase
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Quinone reductase
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Reduced NAD(P)H dehydrogenase
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reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase
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Viologen accepting pyridine nucleotide oxidoreductase
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Vitamin K reductase
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vitamin-K reductase
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WrbA
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WrbA
has NAD(P)H:quinone reductase activity
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NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone
ping-pong mechanism with substrate inhibition
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NAD(P)H:quinone oxidoreductase
A flavoprotein. The enzyme catalyses a two-electron reduction and has a preference for short-chain acceptor quinones, such as ubiquinone, benzoquinone, juglone and duroquinone [6]. The animal, but not the plant, form of the enzyme is inhibited by dicoumarol.
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1,4-benzoquinone + NAD(P)H + H+
1,4-benzoquinol + NAD(P)+
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1,4-benzoquinone + NADH + H+
1,4-benzoquinol + NAD+
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r
1,4-naphthoquinone + NAD(P)H
1,4-naphthohydroquinone + NAD(P)+
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2,3-dihydroxy-5-methyl-1,4-benzoquinone + NAD(P)H
2,3-dihydroxy-5-methyl-1,4-benzoquinol + NAD(P)+
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menadione + NAD(P)H
reduced menadione + NAD(P)+
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NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
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[Fe(CN)6]3- + NAD(P)H
[Fe(CN)6]4- + NAD(P)+
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methyl-1,4-benzoquinone + NADPH + H+
methyl-1,4-benzoquinol + NADP+
two-electron mechanism
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additional information
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additional information
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role of enzyme in protecting against environmental stressors
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additional information
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role of enzyme in protecting against environmental stressors
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additional information
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additional information
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role of enzyme in protecting against environmental stressors
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additional information
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role of enzyme in protecting against environmental stressors
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FMN
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FMN
one molecule per monomer
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0.0058
1,4-benzoquinone
pH 7.2, 37°C
0.0625
NADPH
mutant Y140F, pH 7.5, temperature not specified in the publication
0.0656
NADPH
wild-type, pH 7.5, temperature not specified in the publication
0.0915
NADPH
mutant W139F, pH 7.5, temperature not specified in the publication
0.195
NADPH
mutant W139I, pH 7.5, temperature not specified in the publication
0.225
NADPH
mutant W139A, pH 7.5, temperature not specified in the publication
0.395
NADPH
mutant N143A, pH 7.5, temperature not specified in the publication
0.403
NADPH
mutant N143L, pH 7.5, temperature not specified in the publication
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370
1,4-benzoquinone
pH 7.2, 37°C
18.7
NADPH
mutant N143A, pH 7.5, temperature not specified in the publication
25.2
NADPH
mutant N143L, pH 7.5, temperature not specified in the publication
32.3
NADPH
mutant W139A, pH 7.5, temperature not specified in the publication
34.2
NADPH
wild-type, pH 7.5, temperature not specified in the publication
37.1
NADPH
mutant W139F, pH 7.5, temperature not specified in the publication
45.2
NADPH
mutant Y140F, pH 7.5, temperature not specified in the publication
53.5
NADPH
mutant W139I, pH 7.5, temperature not specified in the publication
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48
NADPH
mutant N143A, pH 7.5, temperature not specified in the publication
63
NADPH
mutant N143L, pH 7.5, temperature not specified in the publication
144
NADPH
mutant W139A, pH 7.5, temperature not specified in the publication
278
NADPH
mutant W139I, pH 7.5, temperature not specified in the publication
407
NADPH
mutant W139F, pH 7.5, temperature not specified in the publication
522
NADPH
wild-type, pH 7.5, temperature not specified in the publication
727
NADPH
mutant Y140F, pH 7.5, temperature not specified in the publication
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160
substrate 2,6-dichlorophenolindophenol, pH 7.2, 37°C
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substrate menadione, pH 7.2, 37°C
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substrate [Fe(CN)6]3-, pH 7.2, 37°C
560
substrate 1,4-naphthoquinone, pH 7.2, 37°C
930
substrate 2,3-dihydroxy-5-methyl-1,4-benzoquinone, pH 7.2, 37°C
990
substrate 1,4-benzoquinone, pH 7.2, 37°C
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6 - 8
more than 95% of maximum activity within this range
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SwissProt
brenda
tryptophan repressor-binding protein
SwissProt
brenda
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21200
4 * 21200, SDS-PAGE
79000
dynamic light scattering
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tetramer
4 * 21200, SDS-PAGE
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with and without FMN using the sitting drop vapor-diffusion technique
crystal structure of WrbA with oxidized FMN
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native enzyme and in complex with NADPH. The N-terminal domain, which adopts the Rossmann fold, provides a platform for NADPH binding, whereas the C-terminal domain, which contains a hydrophobic pocket connected to the NADPH-binding site, plays important roles in substrate binding. Asn143 near the NADPH-binding site is involved in substrate binding and catalysis
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N143A
residue near NADPH-binding site. About 10% of wild-type activity
N143L
residue near NADPH-binding site. About 10% of wild-type activity
W139A
residue near NADPH-binding site. About 30% of wild-type activity
W139F
residue near NADPH-binding site. Activity comparable to wild-type
W139I
residue near NADPH-binding site. About 50% of wild-type activity
Y140A
residue near NADPH-binding site. Almost complete loss of activity
Y140F
residue near NADPH-binding site. Activity comparable to wild-type
Y140I
residue near NADPH-binding site. Almost complete loss of activity
additional information
enzyme knockout mutant, no phenotypes, but N-trichloromethyl-mercapto-4-cyclohexen-1,2-dicarboximide and 8-hydroxyquinoline significantly inhibit growth of mutant relative to growth of wild-type
additional information
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enzyme knockout mutant, no phenotypes, but N-trichloromethyl-mercapto-4-cyclohexen-1,2-dicarboximide and 8-hydroxyquinoline significantly inhibit growth of mutant relative to growth of wild-type
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expression in Escherichia coli
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biotechnology
the flavoprotein WrbA from Escherichia coli represents a new family of multimeric flavodoxin-like proteins implicated in cell protection against oxidative stress, WrbA has NAD(P)H: quinone reductase activity, forms multimers and binds FMN only weakly
additional information
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WrbA bridges flavodoxins and oxidoreductases. WrbA shows a close relationship to mammalian Nqo1
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Patridge, E.V.; Ferry, J.G.
WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase
J. Bacteriol.
188
3498-3506
2006
Escherichia coli (P0A8G6), Escherichia coli, Archaeoglobus fulgidus (P58795), Archaeoglobus fulgidus
brenda
Wolfova, J.; Brynda, J.; Mesters, J.R.; Carey, J.; Grandori, R.; Smatanova, I.K.
Crystallographic study of Escherichia coli flavoprotein WrbA, a new NAD(P)H-dependent quinone oxidoreductase
Mater. Struct. Chem. Biol. Phys. Technol.
15
55-57
2008
Escherichia coli (P0A8G6)
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brenda
Carey, J.; Brynda, J.; Wolfova, J.; Grandori, R.; Gustavsson, T.; Ettrich, R.; Smatanova, I.K.
WrbA bridges bacterial flavodoxins and eukaryotic NAD(P)H:quinone oxidoreductases
Protein Sci.
16
2301-2305
2007
Escherichia coli
brenda
Kim, I.K.; Yim, H.S.; Kim, M.K.; Kim, D.W.; Kim, Y.M.; Cha, S.S.; Kang, S.O.
Crystal structure of a new type of NADPH-dependent quinone oxidoreductase (QOR2) from Escherichia coli
J. Mol. Biol.
379
372-384
2008
Escherichia coli (P39315)
brenda