1.6.5.5: NADPH:quinone reductase
This is an abbreviated version!
For detailed information about NADPH:quinone reductase, go to the full flat file.
Word Map on EC 1.6.5.5
-
1.6.5.5
-
1.6.99.2
-
flavin
-
lens
-
fmn
-
flavoproteins
-
two-electron
-
dicumarol
-
nadph:quinone-acceptor
-
hydroquinone
-
semiquinone
-
bioreductive
-
camel
-
pentaerythritol
-
tetranitrate
-
nadph-quinone
-
taxon-specific
-
2-methyl-1,4-naphthoquinone
-
5-aziridin-1-yl-2,4-dinitrobenzamide
-
morphinone
-
1.6.2.4
-
2,4,6-trinitrotoluene
-
eo9
-
p-hydroxybenzaldehyde
-
9,10-phenanthrenequinone
-
explosives
-
nitroaromatic
-
alpha,beta-unsaturated
-
pastorianus
-
single-electron
-
enones
-
2.5.1.18
-
environmental protection
-
medicine
- 1.6.5.5
-
1.6.99.2
- flavin
- lens
- fmn
- flavoproteins
-
two-electron
- dicumarol
-
nadph:quinone-acceptor
- hydroquinone
- semiquinone
-
bioreductive
- camel
-
pentaerythritol
-
tetranitrate
-
nadph-quinone
-
taxon-specific
- 2-methyl-1,4-naphthoquinone
- 5-aziridin-1-yl-2,4-dinitrobenzamide
- morphinone
-
1.6.2.4
- 2,4,6-trinitrotoluene
- eo9
- p-hydroxybenzaldehyde
- 9,10-phenanthrenequinone
-
explosives
-
nitroaromatic
-
alpha,beta-unsaturated
- pastorianus
-
single-electron
-
enones
-
2.5.1.18
- environmental protection
- medicine
Reaction
Synonyms
ArsH, Dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate) (quinone), DT-diaphorase, EC 1.6.99.2, Flavoprotein NAD(P)H:quinone reductase, Menadione oxidoreductase, Menadione reductase, NAD(P)H dehydrogenase, NAD(P)H dehydrogenase (quinone), NAD(P)H menadione reductase, NAD(P)H quinone reductase, NAD(P)H-quinone dehydrogenase, NAD(P)H-quinone oxidoreductase, NAD(P)H-quinone reductase, NAD(P)H:(quinone-acceptor) oxidoreductase, NAD(P)H:menadione oxidoreductase, NAD(P)H:paraquat diaphorase, NAD(P)H:quinone reductase, NADH-menadione reductase, NADH-menaquinone reductase, NADH:quinone reductase, NADPH DT-diaphorase, NADPH quinone acceptor oxidoreductase, NADPH-dependent quinone reductase, NADPH:azodicarbonyl/quinone reductase, NADPH:quinone oxidoreductase, NADPH:quinone reductase, Naphthoquinone reductase, NfsA, nitroreductase A, old yellow enzyme, ORF 17150, p-Benzoquinone reductase, P1-ZCr, P1-zeta-crystallin, P36, PA0660, Phylloquinone reductase, PtoQOR, QAO, Qor, QorA, Quinone reductase, Reduced NAD(P)H dehydrogenase, TcOYE, TmQR1, VAT-1, vesicle amine transport protein-1, Viologen accepting pyridine nucleotide oxidoreductase, Vitamin K reductase, ZCr, zeta-Crystallin, zeta-crystallin homolog protein, zeta-crystallin/NADPH:quinone oxidoreductase, zeta-Crystallin/quinone reductase, Zta1, Zta1p
ECTree
1.6.5.5 NADPH:quinone reductaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.6.5.5 - NADPH:quinone reductase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,2-naphthoquinone + NADPH + H+
1,2-naphthosemiquinone + NADP+
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
1,2-naphthoquinone + NADPH + H+
? + NADP+
-
the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal
-
-
?
1,4-benzoquinone + NADPH + H+
1,4-benzosemiquinone + NADP+
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
1,4-dihydroxy-9,10-anthraquinone + NADPH + H+
anthracene-1,4,9,10-tetrol + NADP+
-
-
-
-
?
1,8-dihydroxy-9,10-anthraquinone + NADPH + H+
anthracene-1,8,9,10-tetrol + NADP+
-
-
-
-
?
2 1,2-naphthoquinone + NADPH + H+
? + NADP+
-
the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal
-
-
?
2 1,4-benzoquinone + NADPH + H+
2 1,4-benzosemiquinone + NADP+
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 1,4-naphthosemiquinone + NADPH + H+
2 1,4-naphthosemiquinone + NADP+
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 5-hydroxy-1,4-naphthoquinone + NADPH + H+
2 5-hydroxy-1,4-naphthosemiquinone + NADP+
-
i.e. juglone. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 5-hydroxy-2-methyl-1,4-naphthoquinone + NADPH + H+
5-hydroxy-2-methyl-1,4-naphthoquinone + NADP+
-
i.e. plumbagin. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 9,10-phenanthrenequinone + NADPH + H+
? + NADP+
-
70% of the activity with 9,10-phenanthrenequinone
-
-
?
2 decyl-plastoquinone + NADPH + H+
2 decyl-plastosemiquinone + NADP+
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2,3,4,6-tetramethyl-1,4-benzoquinone + NADPH + H+
2,3,4,6-tetramethyl-1,4-benzoquinol + NADP+
-
-
-
?
2,3-dichloro-1,4-naphthoquinone + NADPH + H+
2,3-dichloro-1,4-naphthoquinol + NADP+
-
-
-
-
?
2,3-dimethoxy-5-methyl-1,4-benzoquinone + NADPH + H+
2,3-dimethoxy-5-methyl-1,4-benzoquinol + NADP+
-
-
-
?
2,6-dichlorophenolindophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
the enzyme is 25times more specific for NADPH as a substrate than for NADH
-
-
?
2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+
the enzyme is 25times more specific for NADPH as a substrate than for NADH
-
-
?
2,6-dimethoxy-1,4-benzoquinone + NADPH + H+
2,6-dimethoxy-1,4-benzoquinol + NADP+
-
-
-
?
2,6-dimethyl-1,4-benzoquinone + NADPH + H+
2,6-dimethyl-1,4-benzoquinol + NADP+
-
-
-
-
?
2-hydroxy-1,4-naphthoquinone + NADPH + H+
naphthalene-1,2,4-triol + NADP+
-
-
-
-
?
2-hydroxy-3-methyl-1,4-naphthoquinone + NADPH + H+
3-methylnaphthalene-1,2,4-triol + NADP+
-
-
-
-
?
2-methyl-1,4-benzoquinone + NADPH + H+
2-methyl-1,4-benzoquinol + NADP+
-
-
-
-
?
5,8-dihydroxy-1,4-naphthoquinone + NADPH + H+
5,8-dihydroxy-1,4-naphthoquinol + NADP+
-
-
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH + H+
5-hydroxy-1,4-naphthosemiquinone + NADP+
-
i.e. juglone. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
5-hydroxy-2-methyl-1,4-naphthoquinone + NADPH
5-hydroxy-2-methyl-1,4-naphthoquinol + NADP+
-
i.e. plumbagin, 0.9% of the activity with 1,2-naphthoquinone
-
-
?
5-hydroxy-2-methyl-1,4-naphthoquinone + NADPH + H+
5-hydroxy-2-methyl-1,4-naphthosemiquinone + NADP+
-
i.e. plumbagin. Production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
9,10-anthraquinone-2-sulfonic acid + NADPH + H+
9,10-anthraquinol-2-sulfonic acid + NADP+
-
-
-
-
?
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenesemiquinone + NADP+
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
9,10-phenanthrenequinone + NADPH + H+
? + NADP+
-
the activity with 9,10-phenanthrenequinone and with 1,2-naphthoquinone is equal
-
-
?
methyl-1,4-benzoquinone + NADPH
methyl-1,4-benzoquinol + NADP+
-
20.6% of the activity with 1,2-naphthoquinone
-
-
?
NADPH + H+ + 2 2,5-dimethyl-4-benzoquinone
NADP+ + 2 2,5-dimethyl-4-benzosemiquinone
-
-
-
-
?
NADPH + H+ + 2 2-hydroxy-1,4-naphthoquinone
NADP+ + 2 2-hydroxy-1,4-naphthosemiquinone
-
-
-
-
?
NADPH + H+ + 2 dibromothymoquinone
NADP+ + 2 dibromothymosemiquinone
-
-
-
-
?
NADPH + H+ + komaroviquinone
NADP+ + ?
-
reduction of komaroviquinone to its semiquinone radical. Antichagasic activity of komaroviquinone is due to generation of reactive oxygen species catalyzed by Trypanosoma cruzi old yellow enzyme
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
O2 + NADH + H+
?
the enzyme displays negligible NAD(P)H:oxidase activity
-
-
?
O2 + NADPH + H+
?
the enzyme displays negligible NAD(P)H:oxidase activity
-
-
?
tetramethyl-1,4-benzoquinone + NADPH + H+
tetramethyl-1,4-benzoquinol + NADP+
-
-
-
-
?
1,4-benzoquinone + NADPH
1,4-benzosemiquinone + NADP+
-
15.3% of the activity with 1,2-naphthoquinone
-
-
?
1,4-naphthoquinone + NADPH + H+
1,4-naphthoquinol + NADP+
-
-
-
?
1,4-naphthoquinone + NADPH + H+
1,4-naphthosemiquinone + NADP+
-
-
-
-
?
1,4-naphthoquinone + NADPH + H+
1,4-naphthosemiquinone + NADP+
-
-
-
-
?
1,4-naphthoquinone + NADPH + H+
1,4-naphthosemiquinone + NADP+
-
2.6% of the activity with 1,2-naphthoquinone
-
-
?
1,4-naphthoquinone + NADPH + H+
1,4-naphthosemiquinone + NADP+
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 1,2-naphthoquinone + NADPH + H+
2 1,2-naphthosemiquinone + NADP+
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 9,10-phenanthrenequinone + NADPH + H+
2 9,10-phenanthrenesemiquinone + NADP+
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
2 9,10-phenanthrenequinone + NADPH + H+
2 9,10-phenanthrenesemiquinone + NADP+
-
-
-
-
?
2 9,10-phenanthrenequinone + NADPH + H+
2 9,10-phenanthrenesemiquinone + NADP+
-
very strong reduction activity towards large substrates such as 9,10-phenanthrenequinone. The zeta-crystallin-like quinone oxidoreductase catalyzes one-electron reduction of certain quinones to generate semiquinone
-
-
?
2-methyl-1,4-naphthoquinone + NADPH + H+
2-methyl-1,4-naphthoquinol + NADP+
-
-
-
-
?
2-methyl-1,4-naphthoquinone + NADPH + H+
2-methyl-1,4-naphthoquinol + NADP+
-
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH
5-hydroxy-1,4-naphthosemiquinone + NADP+
-
-
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH
5-hydroxy-1,4-naphthosemiquinone + NADP+
-
i.e. juglone, 12.5% of the activity with 1,2-naphthoquinone
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH + H+
5-hydroxy-1,4-naphthoquinol + NADP+
-
-
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH + H+
5-hydroxy-1,4-naphthoquinol + NADP+
-
-
-
?
9,10-phenanthrenequinone + NADPH
9,10-phenanthrenesemiquinone + NADP+
-
-
-
-
?
9,10-phenanthrenequinone + NADPH
9,10-phenanthrenesemiquinone + NADP+
-
best substrate
-
-
?
9,10-phenanthrenequinone + NADPH
9,10-phenanthrenesemiquinone + NADP+
-
-
-
-
?
9,10-phenanthrenequinone + NADPH
9,10-phenanthrenesemiquinone + NADP+
-
50% of the activity with 1,2-naphthoquinone
-
-
?
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenequinol + NADP+
-
-
-
-
?
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenequinol + NADP+
-
-
-
?
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenequinol + NADP+
one-electron reduction mechanism. Concomitantly with NADPH consumption, generation of superoxide is observed
-
-
?
dichlorophenolindophenol + NADPH + H+
reduced dichlorophenolindophenol + NADP+
-
-
-
-
?
dichlorophenolindophenol + NADPH + H+
reduced dichlorophenolindophenol + NADP+
-
production of semiquinone by univalent catalysts is detectable by the reduction of ferricytochrome c by the semiquinone to ferrocytochrome c
-
-
?
dichlorophenolindophenol + NADPH + H+
reduced dichlorophenolindophenol + NADP+
-
-
-
-
?
menadione + NADPH + H+
menadiol + NADP+
-
-
under aerobic conditions, menadiol is readily oxidized to menadione by two 1-electron steps producing the semiquinone and the parent quinone with concomitant production of superoxide anion, which leads to generation of hydroxyl radicals
-
?
NADPH + H+ + 2 quinone
NADP+ + 2 semiquinone
-
the catalytic cycle of ArsH consists of the acceptance of two electrons from NADPH to reduce the flavin cofactor (reductive half-reaction) and the transfer of these electrons to an acceptor (oxidative half-reaction)
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
3.8% of the activity with 1,2-naphthoquinone
-
-
?
additional information
?
-
-
no activity with: phylloquinone (vitamin K1), menaquinone (vitamin K2), menadione (vitamin K3) and ferricyanide. Preference for o-quinones over p-quinones, and the inability to recognize menadione and ferricyanide as substrates, clearly distinguishe P1-ZCr and guinea-pig ZCr from the flavin-containing NAD(P)H-quinone oxidoreductases in plants and animals. P1-ZCr also catalyzed the divalent reduction of diamide to 1,2-bis(N,N-dimethylcarbamoyl)hydrazine, with a kcat comparable with that for quinones. Two other azodicarbonyl compounds also served as substrates of P1-ZCr. Guinea-pig ZCr, however, did not catalyze the azodicarbonyl reduction. Hence, plant ZCr is distinct from mammalian ZCr, and can be referred to as NADPH:azodicarbonyl/quinone reductase. The quinone-reducing reaction is accompanied by radical chain reactions to produce superoxide radicals, while the azodicarbonyl reducing reaction is not
-
-
?
additional information
?
-
-
no activity with menadione and 9,10-anthraquinone
-
-
?
additional information
?
-
-
inactive with: menadione, ubiquinone, 9,10-anthraquinone, vitamin K1, vitamin K2
-
-
?
additional information
?
-
-
although in the lens the enzyme is considered to be a crystallin, or lens structural protein, because of its high abundance its enzymatic activity and expression at catalytic levels in other tissues of various species suggest that it has a fundamental physiological role outside the lens, perhaps in the detoxification of xenobiotics
-
-
?
additional information
?
-
-
no activity with: phylloquinone (vitamin K1), menaquinone (vitamin K2), menadione (vitamin K3), ferricytochrome and ferricyanide. Preference for o-quinones over p-quinones, and the inability to recognize menadione and ferricyanide as substrates, clearly distinguishe Arabidopsis thaliana P1-ZCr and guinea-pig ZCr from the flavin-containing NAD(P)H-quinone oxidoreductases in plants and animals
-
-
?
additional information
?
-
-
NADPH-dependent reduction of quinones and nitroaromatic compounds by NfsA, overview. The reactivity of nitroaromatic compounds (log kcat/Km) follows a linear dependence on their single-electron reduction potential, indicating a limited role for compound structure or active site flexibility in their reactivity. The reactivity of quinones is lower than that of nitroaromatics having similar single-electron reduction potential values, except for the significantly enhanced reactivity of 2-OH-1,4-naphthoquinones. The reduction of quinones by NfsA is most consistent with a single-step (H-) hydride transfer mechanism, quantitative analysis of two-electron reduction of quinones and nitroaromatics, overview
-
-
?
additional information
?
-
coenzyme Q and tetracycline may be used as electron acceptors, but with much lower specific activities than menadione. Nitro compounds dinitrotoluene, 7-nitrocoumarin, and metronidazole can be used as electron acceptors
-
-
-
additional information
?
-
-
coenzyme Q and tetracycline may be used as electron acceptors, but with much lower specific activities than menadione. Nitro compounds dinitrotoluene, 7-nitrocoumarin, and metronidazole can be used as electron acceptors
-
-
-
additional information
?
-
coenzyme Q and tetracycline may be used as electron acceptors, but with much lower specific activities than menadione. Nitro compounds dinitrotoluene, 7-nitrocoumarin, and metronidazole can be used as electron acceptors
-
-
-
additional information
?
-
-
although in the lens the enzyme is considered to be a crystallin, or lens structural protein, because of its high abundance its enzymatic activity and expression at catalytic levels in other tissues of various species suggest that it has a fundamental physiological role outside the lens, perhaps in the detoxification of xenobiotics
-
-
?
additional information
?
-
-
the human and yeast enzymes specifically bind to adenine-uracil rich elements (ARE) in RNA, indicating that both enzymes are ARE-binding proteins and that this property has been conserved in zeta-crystallins throughout evolution. This supports a role for zeta-crystallins as trans-acting factors that could regulate the turnover of certain mRNAs
-
-
?
additional information
?
-
-
enzyme reduces ortho-quinones in the presence of NADPH but is not active with 2-alkenals
-
-
?
additional information
?
-
the enzyme does not exhibit nitronate monooxygenase activity (no activity with propionate 3-nitronate, 3-nitropropionate, nitroethane, 2-nitropropane, ethylnitronate, or propyl-2-nitronate) and does not turn over with methyl red, consistent with a lack of azoreductase activity
-
-
-
additional information
?
-
-
the human and yeast enzymes specifically bind to adenine-uracil rich elements (ARE) in RNA, indicating that both enzymes are ARE-binding proteins and that this property has been conserved in zeta-crystallins throughout evolution. This supports a role for zeta-crystallins as trans-acting factors that could regulate the turnover of certain mRNAs
-
-
?
additional information
?
-
-
enzyme reduces ortho-quinones in the presence of NADPH but is not active with 2-alkenals
-
-
?
additional information
?
-
-
although the enzyme is able to stabilize the anionic semiquinone form of the FMN, reduction of quinones involves the hydroquinone form of the flavin cofactor, and the enzymatic reaction occurs through a ping pong-type mechanism. ArsH is able to catalyze one-electron reactions (oxygen and cytocrome c reduction), involving the FMN semiquinone form, but with lower efficiency
-
-
?
additional information
?
-
QR1 catalyzes the univalent reduction of quinones to semiquinone radicals
-
-
?
additional information
?
-
-
QR1 catalyzes the univalent reduction of quinones to semiquinone radicals
-
-
?
