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1,2-naphthoquinone + NADPH
1,2-naphthoquinol + NADP+
1,2-naphthoquinone + NADPH + H+
1,2-naphthoquinol + NADP+
-
-
-
?
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
1,4-benzosemiquinone + NADP+
1,4-benzoquinone + NADPH + H+
1,4-benzoquinol + NADP+
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+
-
-
-
-
?
1,4-naphthoquinone + NADPH + H+
1,4-naphthoquinol + NADP+
1,4-naphthoquinone + NADPH + H+
1,4-naphthosemiquinone + NADP+
1,8-dihydroxy-9,10-anthraquinone + NADPH + H+
anthracene-1,8,9,10-tetrol + NADP+
-
-
-
-
?
2 1,2-naphthoquinone + NADPH + H+
2 1,2-naphthosemiquinone + 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-benzoquinone + NADPH + H+
? + NADP+
-
weak activity
-
-
?
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+
2 9,10-phenanthrenesemiquinone + NADP+
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-hexenal + NADPH
hexanal + 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+
-
-
-
-
?
2-methyl-1,4-naphthoquinone + NADPH + H+
2-methyl-1,4-naphthoquinol + NADP+
2-nonenal + NADPH
nonanal + NADP+
-
-
-
?
2-pentenal + NADPH
pentanal + NADP+
-
-
-
?
3-buten-2-one + NADPH
2-butanone + NADP+
-
-
-
?
3-nonen-2-one + NADPH
2-nonanone + NADP+
-
-
-
?
3-penten-2-one + NADPH
2-pentanone + NADP+
-
-
-
?
4-hydroxy-2-hexenal + NADPH
4-hydroxy-hexanal + NADP+
-
-
-
?
4-hydroxy-2-nonenal + NADPH
4-hydroxy-nonanal + NADP+
-
-
-
?
5,8-dihydroxy-1,4-naphthoquinone + NADPH + H+
5,8-dihydroxy-1,4-naphthoquinol + NADP+
-
-
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH
5-hydroxy-1,4-naphthosemiquinone + NADP+
5-hydroxy-1,4-naphthoquinone + NADPH + H+
5-hydroxy-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-1,4-naphthoquinone + NADPH + H+
?
-
i.e. juglone
-
-
?
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
9,10-phenanthrenesemiquinone + NADP+
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenequinol + 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
-
-
?
dichlorophenolindophenol + NADPH + H+
reduced dichlorophenolindophenol + NADP+
ferricytochrome + NADPH + H+
ferrocytochrome + NADP+
-
-
-
-
?
menadione + NADPH + H+
menadiol + NADP+
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 anthraquinone-2-sulfonate
NADP+ + ?
-
-
-
-
?
NADPH + H+ + 2 coenzyme Q10
NADP+ + ?
-
-
-
-
?
NADPH + H+ + 2 dibromothymoquinone
NADP+ + 2 dibromothymosemiquinone
-
-
-
-
?
NADPH + H+ + 2 duroquinone
NADP+ + 2 durosemiquinone
-
-
-
-
?
NADPH + H+ + 2 menadione
NADP+ + ?
-
-
-
-
?
NADPH + H+ + 2 quinone
NADP+ + 2 semiquinone
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+ + menadione
NADP+ + ?
-
-
-
-
?
NADPH + H+ + nifurtimox
NADP+ + ?
-
-
-
-
?
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
-
-
?
propenal + NADPH
propanal + NADP+
-
-
-
?
riboflavin + NADPH + H+
? + NADP+
-
-
-
-
?
tetramethyl-1,4-benzoquinone + NADPH + H+
tetramethyl-1,4-benzoquinol + NADP+
-
-
-
-
?
additional information
?
-
1,2-naphthoquinone + NADPH
1,2-naphthoquinol + NADP+
-
-
-
-
?
1,2-naphthoquinone + NADPH
1,2-naphthoquinol + NADP+
-
-
-
-
?
1,4-benzoquinone + NADPH
1,4-benzosemiquinone + NADP+
-
-
-
-
?
1,4-benzoquinone + NADPH
1,4-benzosemiquinone + NADP+
-
15.3% of the activity with 1,2-naphthoquinone
-
-
?
1,4-benzoquinone + NADPH + H+
1,4-benzoquinol + NADP+
-
-
-
-
?
1,4-benzoquinone + NADPH + H+
1,4-benzoquinol + NADP+
-
-
-
?
1,4-naphthoquinone + NADPH + H+
1,4-naphthoquinol + NADP+
-
-
-
-
?
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 1,2-naphthoquinone + NADPH + H+
2 1,2-naphthosemiquinone + NADP+
-
-
-
-
?
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+
-
-
-
?
menadione + NADPH + H+
menadiol + 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
-
?
menadione + NADPH + H+
menadiol + NADP+
-
-
-
?
NADPH + H+ + 2 quinone
NADP+ + 2 semiquinone
-
-
-
-
?
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
-
-
?
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Acidosis
Role of deadenylation and AUF1 binding in the pH-responsive stabilization of glutaminase mRNA.
Acidosis
Zeta-crystallin mediates the acid pH-induced increase of BSC1 cotransporter mRNA stability.
Acidosis
Zeta-crystallin: a tale of two cells.
Breast Neoplasms
Mammalian protein homologous to VAT-1 of Torpedo californica: isolation from Ehrlich ascites tumor cells, biochemical characterization, and organization of its gene.
Carcinogenesis
DT-diaphorase: possible roles in cancer chemotherapy and carcinogenesis.
Carcinogenesis
Long term effects of benzo(a)pyrene on the activity of NAD(P)H:quinone reductase in the forestomach and glandular stomach of ICR/Ha mice.
Carcinoma
Caffeine, aminoimidazolecarboxamide and dicoumarol, inhibitors of NAD(P)H dehydrogenase (quinone) (DT diaphorase), prevent both the cytotoxicity and DNA interstrand crosslinking produced by 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954) in Walker cells.
Carcinoma
Role of NAD(P)H:quinone oxidoreductase (DT-diaphorase) in cytotoxicity and induction of DNA damage by streptonigrin.
Carcinoma
The differences in kinetics of rat and human DT diaphorase result in a differential sensitivity of derived cell lines to CB 1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide)
Carcinoma
The role of NAD(P)H:quinone oxidoreductase in quinone-mediated p21 induction in human colon carcinoma cells.
Carcinoma, Ehrlich Tumor
Mammalian protein homologous to VAT-1 of Torpedo californica: isolation from Ehrlich ascites tumor cells, biochemical characterization, and organization of its gene.
Carcinoma, Hepatocellular
1,2-Dithiol-3-thione analogs: effects on NAD(P)H:quinone reductase and glutathione levels in murine hepatoma cells.
Carcinoma, Hepatocellular
Direct determination of functional activity of cytochrome P-4501A1 and NADPH DT-diaphorase in hepatoma cell lines using noninvasive scanning laser cytometry.
Carcinoma, Hepatocellular
Induction of NAD(P)H:quinone reductase in murine hepatoma cells by phenolic antioxidants, azo dyes, and other chemoprotectors: a model system for the study of anticarcinogens.
Carcinoma, Hepatocellular
Induction of NADPH:quinone oxidoreductase in murine hepatoma cells by methylsulfinyl isothiocyanates: methyl chain length-activity study.
Carcinoma, Hepatocellular
Mechanisms of induction of enzymes that protect against chemical carcinogenesis.
Carcinoma, Hepatocellular
Mercurials and dimercaptans: synergism in the induction of chemoprotective enzymes.
Carcinoma, Hepatocellular
Rapid detection of inducers of enzymes that protect against carcinogens.
Carcinoma, Hepatocellular
The p53-inducible gene 3 involved in flavonoid-induced cytotoxicity through the reactive oxygen species-mediated mitochondrial apoptotic pathway in human hepatoma cells.
Cataract
A guinea-pig hereditary cataract contains a splice-site deletion in a crystallin gene.
Cataract
Assignment of the zeta-crystallin gene (CRYZ) to human chromosome 1p22-p31 and identification of restriction fragment length polymorphisms.
Cataract
Association of hereditary cataracts in strain 13/N guinea-pigs with mutation of the gene for zeta-crystallin.
Cataract
Expression of recombinant zeta-crystallin in Escherichia coli with the help of GroEL/ES and its purification.
Cataract
Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase.
Cataract
Mutant zeta-crystallin from guinea-pig hereditary cataracts has altered structural and enzymatic properties.
Cataract
On the nature of hereditary cataract in strain 13/N guinea pigs.
Cataract
The transcripts of zeta-crystallin, a lens protein related to the alcohol dehydrogenase family, are altered in a guinea-pig hereditary cataract.
Cataract
Zeta-crystallin catalyzes the reductive activation of 2,4,6-trinitrotoluene to generate reactive oxygen species: a proposed mechanism for the induction of cataracts.
Colonic Neoplasms
NF-kappaB activation by the chemopreventive dithiolethione oltipraz is exerted through stimulation of MEKK3 signaling.
Glioblastoma
Vesicle amine transport protein-1 (VAT-1) is upregulated in glioblastomas and promotes migration.
Glioma
Vesicle amine transport protein-1 (VAT-1) is upregulated in glioblastomas and promotes migration.
Infections
Differential regulation of wheat quinone reductases in response to powdery mildew infection.
Lens Diseases
A guinea-pig hereditary cataract contains a splice-site deletion in a crystallin gene.
Leukemia
{zeta}-Crystallin is a bcl-2 mRNA binding protein involved in bcl-2 overexpression in T-cell acute lymphocytic leukemia.
Neoplasms
Bioactive S-alk(en)yl cysteine sulfoxide metabolites in the genus Allium: the chemistry of potential therapeutic agents.
Neoplasms
Cigarette smoking is a determinant of DT-diaphorase gene expression in human non-small cell lung carcinoma.
Neoplasms
Cytotoxicity of RH1: NAD(P)H:quinone acceptor oxidoreductase (NQO1)-independent oxidative stress and apoptosis induction.
Neoplasms
Detection of (NAD(P)H:Quinone oxidoreductase-1, EC 1.6.99.2) 609C-->T and 465C-->T polymorphisms in formalin-fixed, paraffin-embedded human tumour tissue using PCR-RFLP.
Neoplasms
Differential induction of Cyp1a1, Cyp1b1, Ahd4, and Nmo1 in murine skin tumors and adjacent normal epidermis by ligands of the aryl hydrocarbon receptor.
Neoplasms
DT-diaphorase in morbidly obese patients.
Neoplasms
DT-diaphorase: possible roles in cancer chemotherapy and carcinogenesis.
Neoplasms
Enzymology of the reduction of the potent benzotriazine-di-N-oxide hypoxic cell cytotoxin SR 4233 (WIN 59075) by NAD(P)H: (quinone acceptor) oxidoreductase (EC 1.6.99.2) purified from Walker 256 rat tumour cells.
Neoplasms
Establishment of an isogenic human colon tumor model for NQO1 gene expression: application to investigate the role of DT-diaphorase in bioreductive drug activation in vitro and in vivo.
Neoplasms
Fisetin induces transcription of NADPH:quinone oxidoreductase gene through an antioxidant responsive element-involved activation.
Neoplasms
Immunodetection of NAD(P)H:quinone oxidoreductase 1 (NQO1) in human tissues.
Neoplasms
Immunohistochemical localization of NAD(P)H:quinone oxidoreductase in conjunctival melanomas and primary acquired melanosis.
Neoplasms
Mammalian protein homologous to VAT-1 of Torpedo californica: isolation from Ehrlich ascites tumor cells, biochemical characterization, and organization of its gene.
Neoplasms
Neocarzilin A Is a Potent Inhibitor of Cancer Cell Motility Targeting VAT-1 Controlled Pathways.
Neoplasms
Nitroreductase, a near-infrared reporter platform for in vivo time-domain optical imaging of metastatic cancer.
Neoplasms
Nitroreductase: a prodrug-activating enzyme for cancer gene therapy.
Neoplasms
Pharmacological properties of a new aziridinylbenzoquinone, RH1 (2,5-diaziridinyl-3-(hydroxymethyl)-6-methyl-1,4-benzoquinone), in mice.
Neoplasms
Role of redox cycling and activation by DT-diaphorase in the cytotoxicity of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB-1954) and its analogs.
Neoplasms
Targeting glutamine metabolism sensitizes pancreatic cancer to PARP-driven metabolic catastrophe induced by ß-lapachone.
Neoplasms
Xenobiotic metabolizing enzymes in genetically and chemically initiated mouse liver tumors.
Neoplasms
Zeta-crystallin: a moonlighting player in cancer.
Pancreatic Neoplasms
Dicumarol inhibition of NADPH:quinone oxidoreductase induces growth inhibition of pancreatic cancer via a superoxide-mediated mechanism.
Papilloma
Differential induction of Cyp1a1, Cyp1b1, Ahd4, and Nmo1 in murine skin tumors and adjacent normal epidermis by ligands of the aryl hydrocarbon receptor.
Paralysis
The murine aromatic hydrocarbon responsiveness locus: a comparison of receptor levels and several inducible enzyme activities among recombinant inbred lines.
Precursor T-Cell Lymphoblastic Leukemia-Lymphoma
{zeta}-Crystallin is a bcl-2 mRNA binding protein involved in bcl-2 overexpression in T-cell acute lymphocytic leukemia.
Prostatic Hyperplasia
VAT-1 is a novel pathogenic factor of progressive benign prostatic hyperplasia.
Prostatic Neoplasms
VAT-1 is a novel pathogenic factor of progressive benign prostatic hyperplasia.
Sarcoma
Targeting glutamine metabolism sensitizes pancreatic cancer to PARP-driven metabolic catastrophe induced by ß-lapachone.
Urinary Bladder Neoplasms
A novel strategy for NQO1 (NAD(P)H:quinone oxidoreductase, EC 1.6.99.2) mediated therapy of bladder cancer based on the pharmacological properties of EO9.
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Rao, P.V.; Krishna, C.M.; Zigler, J.S.
Identification and characterization of the enzymatic activity of zeta-Crystallin from guinea pig lens
J. Biol. Chem.
267
96-102
1992
Cavia porcellus
brenda
Duhaiman, A.S.; Rabbani, N.
Involvement of a disulfide bridge in catalytic activity of camel lens zeta-crystallin
Biochem. Biophys. Res. Commun.
221
229-233
1996
Camelus dromedarius
brenda
Duhaiman, A.S.; Rabbani, N.; AlJafari, A.A.; Alhomida, A.S.
Purification and characterization of zeta-crystallin from the camel lens
Biochem. Biophys. Res. Commun.
215
632-640
1995
Camelus dromedarius
brenda
Duhaiman, A.S.
Inhibition of camel lens zeta-crystallin/NADPH:quinone oxidoreductase activity by cibacron blue
J. Enzyme Inhib.
10
263-269
1996
Camelus dromedarius
brenda
Duhaiman, A.S.
Camel lens zeta-crystallin kinetics and its inhibition by dicoumarol
Biochem. Mol. Biol. Int.
38
251-258
1996
Camelus dromedarius
brenda
Abdulaziz, A.A A.; Riskuwa, A.S.; Duhaiman, A.S.
Inhibition of camel lens zeta-crystallin/NADPH:quinone oxidoreductase activity by chloranilic acid
Biochem. Mol. Biol. Int.
41
415-421
1997
Camelus dromedarius
brenda
Rao, P.V.; Zigler, J.S.
Purification and characterization of zeta-crystallin/quinone reductase from guinea pig liver
Biochim. Biophys. Acta
1117
315-320
1992
Cavia porcellus, Homo sapiens
brenda
Rabbani, N.; Duhaiman, A.S.
Inhibition of camel lens zeta-crystallin/NADPH:quinone oxidoreductase by pyridoxal-5'-phosphate
Biochim. Biophys. Acta
1388
175-180
1998
Camelus dromedarius
brenda
Duhaiman, A.S.
Inhibition of zeta-crystallin by coumarins: a structure-activity study
J. Protein Chem.
15
261-264
1996
Camelus dromedarius
brenda
Duhaiman, A.S.
Kinetic properties of camel lens zeta-crystallin
Int. J. Biochem. Cell Biol.
28
1163-1168
1996
Camelus dromedarius
brenda
Rao, P.V.; Gonzalez, P.; Persson, B.; Jornvall, H.; Garland, D.; Zigler, J.S.
Guinea pig and bovine zeta-crystallins have distinct functional characteristics highlighting replacements in otherwise similar structures
Biochemistry
36
5353-5362
1997
Bos taurus, Cavia porcellus
brenda
Shimomura, Y.; Kakuta, Y.; Fukuyama, K.
Crystal structures of the quinone oxidoreductase from Thermus thermophilus HB8 and its complex with NADPH: Implication for NADPH and substrate recognition
J. Bacteriol.
185
4211-4218
2003
Thermus thermophilus (Q8L3C8), Thermus thermophilus HB8 / ATCC 27634 / DSM 579 (Q8L3C8)
brenda
Uchiyama, N.; Kabututu, Z.; Kubata, B.K.; Kiuchi, F.; Ito, M.; Nakajima-Shimada, J.; Aoki, T.; Ohkubo, K.; Fukuzumi, S.; Martin, S.K.; Honda, G.; Urade, Y.
Antichagasic activity of komaroviquinone is due to generation of reactive oxygen species catalyzed by Trypanosoma cruzi old yellow enzyme
Antimicrob. Agents Chemother.
49
5123-5126
2005
Trypanosoma cruzi
brenda
Greenshields, D.L.; Liu, G.; Selvaraj, G.; Wei, Y.
Differential regulation of wheat quinone reductases in response to powdery mildew infection
Planta
222
867-875
2005
Triticum monococcum (Q56D13), Triticum monococcum
brenda
Pan, X.; Zhang, H.; Gao, Y.; Li, M.; Chang, W.
Crystal structures of Pseudomonas syringae pv. tomato DC3000 quinone oxidoreductase and its complex with NADPH.
Biochem. Biophys. Res. Commun.
390
597-602
2009
Pseudomonas syringae
brenda
Fernandez, M.R.; Porte, S.; Crosas, E.; Barbera, N.; Farres, J.; Biosca, J.A.; Pares, X.
Human and yeast zeta-crystallins bind AU-rich elements in RNA
Cell. Mol. Life Sci.
64
1419-1427
2007
Saccharomyces cerevisiae, Homo sapiens
brenda
Porte, S.; Crosas, E.; Yakovtseva, E.; Biosca, J.A.; Farres, J.; Fernandez, M.R.; Pares, X.
MDR quinone oxidoreductases: the human and yeast zeta-crystallins
Chem. Biol. Interact.
178
288-294
2009
Saccharomyces cerevisiae (P38230), Saccharomyces cerevisiae, Homo sapiens (Q08257), Homo sapiens
brenda
Mano, J.; Babiychuk, E.; Belles-Boix, E.; Hiratake, J.; Kimura, A.; Inze, D.; Kushnir, S.; Asada, K.
A novel NADPH:diamide oxidoreductase activity in Arabidopsis thaliana P1 zeta-crystallin
Eur. J. Biochem.
267
3661-3671
2000
Arabidopsis thaliana, Cavia porcellus
brenda
Huang, Q.L.; Du, X.Y.; Stone, S.H.; Amsbaugh, D.F.; Datiles, M.; Hu, T.S.; Zigler, J.S.
Association of hereditary cataracts in strain 13/N guinea-pigs with mutation of the gene for zeta-crystallin
Exp. Eye Res.
50
317-325
1990
Cavia porcellus, Cavia porcellus 13/N
brenda
Simpanya, M.F.; Leverenz, V.R.; Giblin, F.J.
Expression and purification of his-tagged recombinant mouse zeta-crystallin
Protein Expr. Purif.
69
147-152
2010
Mus musculus
brenda
Nutter, L.M.; Ngo, E.O.; Fisher, G.R.; Gutierrez, P.L.
DNA strand scission and free radical production in menadione-treated cells. Correlation with cytotoxicity and role of NADPH quinone acceptor oxidoreductase
J. Biol. Chem.
267
2474-2479
1992
Homo sapiens
brenda
Maruyama, A.; Kumagai, Y.; Morikawa, K.; Taguchi, K.; Hayashi, H.; Ohta, T.
Oxidative-stress-inducible qorA encodes an NADPH-dependent quinone oxidoreductase catalysing a one-electron reduction in Staphylococcus aureus
Microbiology
149
389-398
2003
Staphylococcus aureus (A0A0H3JVE7), Staphylococcus aureus
brenda
Hervas, M.; Lopez-Maury, L.; Leon, P.; Sanchez-Riego, A.M.; Florencio, F.J.; Navarro, J.A.
ArsH from the cyanobacterium Synechocystis sp. PCC 6803 is an efficient NADPH-dependent quinone reductase
Biochemistry
51
1178-1187
2012
Synechocystis sp.
brenda
Porte, S.; Moeini, A.; Reche, I.; Shafqat, N.; Oppermann, U.; Farres, J.; Pares, X.
Kinetic and structural evidence of the alkenal/one reductase specificity of human zeta-crystallin
Cell. Mol. Life Sci.
68
1065-1077
2011
Homo sapiens (Q08257)
brenda
Valiauga, B.; Williams, E.M.; Ackerley, D.F.; Cenas, N.
Reduction of quinones and nitroaromatic compounds by Escherichia coli nitroreductase A (NfsA) Characterization of kinetics and substrate specificity
Arch. Biochem. Biophys.
614
14-22
2017
Escherichia coli
brenda
Alharbi, I.; Khan, M.; Rabbani, N.; Al-Senaidy, A.; Ismael, M.; Ayoub, M.
Inhibition of NADPH quinone oxidoreductase activity of camel lens zeta-crystallin by colchicine
Curr. Enzyme Inhib.
10
137-142
2014
Camelus sp.
-
brenda
Crosas, E.; Sumoy, L.; Gonzalez, E.; Diaz, M.; Bartolome, S.; Farres, J.; Pares, X.; Biosca, J.A.; Fernandez, M.R.
The yeast zeta-crystallin/NADPH quinone oxidoreductase (Zta1p) is under nutritional control by the target of rapamycin pathway and is involved in the regulation of argininosuccinate lyase mRNA half-life
FEBS J.
282
1953-1964
2015
Saccharomyces cerevisiae
brenda
Reis, R.A.G.; Salvi, F.; Williams, I.; Gadda, G.
Kinetic investigation of a presumed nitronate monooxygenase from Pseudomonas aeruginosa PAO1 establishes a new class of NAD(P)H quinone reductases
Biochemistry
58
2594-2607
2019
Pseudomonas aeruginosa (Q9I5R1)
brenda
Mueller, J.; Heller, M.; Uldry, A.C.; Braga, S.; Mueller, N.
Nitroreductase activites in Giardia lamblia ORF 17150 encodes a quinone reductase with nitroreductase activity
Pathogens
10
129
2021
Giardia intestinalis (A8BSH8), Giardia intestinalis, Giardia intestinalis ATCC 50803 (A8BSH8)
brenda
Kim, S.; Mori, T.; Chek, M.; Furuya, S.; Matsumoto, K.; Yajima, T.; Ogura, T.; Hakoshima, T.
Structural insights into vesicle amine transport-1 (VAT-1) as a member of the NADPH-dependent quinone oxidoreductase family
Sci. Rep.
11
2120
2021
Homo sapiens (A0A024R1Z6), Homo sapiens
brenda
Shukla, V.; Asthana, S.; Yadav, S.; Rajput, V.S.; Tripathi, A.
Emodin inhibited NADPH-quinone reductase competitively and induced cytotoxicity in rat primary hepatocytes
Toxicon
188
117-121
2020
Rattus norvegicus
brenda