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Information on EC 1.6.5.2 - NAD(P)H dehydrogenase (quinone) and Organism(s) Escherichia coli and UniProt Accession P0A8G6

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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.
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This record set is specific for:
Escherichia coli
UNIPROT: P0A8G6
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Word Map
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NADPH:quinone oxidoreductase
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azoreductase
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dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone)
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diaphorase
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DT-diaphorase
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DTD
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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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QR1
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QR2
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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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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone
show the reaction diagram
ping-pong mechanism with substrate inhibition
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-20-6
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-benzoquinone + NAD(P)H + H+
1,4-benzoquinol + NAD(P)+
show the reaction diagram
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?
1,4-benzoquinone + NADH + H+
1,4-benzoquinol + NAD+
show the reaction diagram
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r
1,4-naphthoquinone + NAD(P)H
1,4-naphthohydroquinone + NAD(P)+
show the reaction diagram
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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)+
show the reaction diagram
-
-
-
?
menadione + NAD(P)H
reduced menadione + NAD(P)+
show the reaction diagram
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?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
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?
[Fe(CN)6]3- + NAD(P)H
[Fe(CN)6]4- + NAD(P)+
show the reaction diagram
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?
methyl-1,4-benzoquinone + NADPH + H+
methyl-1,4-benzoquinol + NADP+
show the reaction diagram
two-electron mechanism
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?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0058
1,4-benzoquinone
pH 7.2, 37°C
0.014
NADH
pH 7.2, 37°C
0.17
NADPH
pH 7.2, 37°C
0.0625 - 0.403
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
370
1,4-benzoquinone
pH 7.2, 37°C
8.9
NADH
pH 7.2, 37°C
6
NADPH
pH 7.2, 37°C
18.7 - 53.5
NADPH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
48 - 727
NADPH
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
160
substrate 2,6-dichlorophenolindophenol, pH 7.2, 37°C
430
substrate menadione, pH 7.2, 37°C
50
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
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
more than 95% of maximum activity within this range
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21000
SDS-PAGE
21200
4 * 21200, SDS-PAGE
79000
dynamic light scattering
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
4 * 21200, SDS-PAGE
tetramer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
for crystallization
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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)
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team