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Information on EC 1.6.5.2 - NAD(P)H dehydrogenase (quinone) and Organism(s) Mus musculus and UniProt Accession Q64669
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1.6.5.2 NAD(P)H dehydrogenase (quinone)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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Word Map
- 1.6.5.2
- s-transferase
- dismutase
- oxygenase-1
- catalase
- gst
-
chemopreventive
-
detoxify
-
two-electron
- dicoumarol
-
2-related
-
erythroid
-
cytoprotective
- hydroquinone
-
bioreductive
- mitomycin
- sulforaphane
- isothiocyanate
- cyp1a1
- nitroreductase
-
decolor
- hepa
-
one-electron
-
glutamate-cysteine
-
benzoapyrene
-
nrf2-mediated
- semiquinone
-
chemoprotective
-
nadph-cytochrome
-
nrf2-dependent
-
kelch-like
-
drug-metabolizing
-
nf-e2-related
-
anticarcinogenic
- medicine
- glucosinolates
- plastoquinone
- nadph-d
-
textile
-
ech-associated
- 3-methylcholanthrene
-
xenobiotic-metabolizing
-
nrf2-are
-
udp-glucuronosyltransferase
-
erythroid-derived
-
ethoxyresorufin
- beta-naphthoflavone
- tert-butylhydroquinone
-
ferredoxin-nadp+
-
peitc
- pharmacology
- drug development
- analysis
- degradation
- methemoglobinemia
-
pentoxyresorufin
- biotechnology
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
azoreductase
-
-
-
-
dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone)
-
-
-
-
diaphorase
-
-
-
-
DT-diaphorase
DTD
-
-
-
-
flavoprotein NAD(P)H-quinone reductase
-
-
-
-
Menadione oxidoreductase
-
-
-
-
Menadione reductase
-
-
-
-
NAD(P)H dehydrogenase
-
-
-
-
NAD(P)H menadione reductase
-
-
-
-
NAD(P)H-quinone dehydrogenase
-
-
-
-
NAD(P)H-quinone oxidoreductase
-
-
-
-
NAD(P)H: (quinone-acceptor)oxidoreductase
-
-
-
-
NAD(P)H: menadione oxidoreductase
-
-
-
-
NADH-menadione reductase
-
-
-
-
Naphthoquinone reductase
-
-
-
-
p-Benzoquinone reductase
-
-
-
-
Phylloquinone reductase
-
-
-
-
QR1
QR2
-
-
-
-
Quinone reductase
Reduced NAD(P)H dehydrogenase
-
-
-
-
reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase
-
-
-
-
Viologen accepting pyridine nucleotide oxidoreductase
-
-
-
-
Vitamin K reductase
vitamin-K reductase
-
-
-
-
DT-diaphorase
-
-
-
-
QR1
-
-
-
-
Quinone reductase
-
-
-
-
Vitamin K reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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
9032-20-6
-
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
3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide + NAD(P)H
reduced 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide + NAD(P)+
-
-
-
-
?
5-(1-aziridinyl)-3-(hydroxymethyl)-2-(3-hydroxy-1-propenyl)-1-methyl-1H-indole-4,7-dione + NAD(P)H
5-(1-aziridinyl)-3-(hydroxymethyl)-2-(3-hydroxy-1-propenyl)-1-methyl-1H-indole-4,7-diol + NAD(P)+
-
-
-
?
5-(aziridin-1-yl)-2,4-dinitrobenzamide + NAD(P)H
5-(aziridin-1-yl)-4-hydroxylamino-2-nitrobenzamide + NAD(P)+
-
-
-
?
5-(aziridin-1-yl)-2,4-dinitrobenzamide + reduced dihydronicotineamide riboside
5-(aziridin-1-yl)-4-hydroxylamino-2-nitrobenzamide + oxidized dihydronicotineamide riboside
-
-
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
2-methyl-1,4-naphthoquinone + NAD(P)H
2-methyl-1,4-naphthoquinol + NAD(P)+
-
-
-
-
?
2-methyl-1,4-naphthoquinone + NAD(P)H
2-methyl-1,4-naphthoquinol + NAD(P)+
-
-
-
?
2-methyl-1,4-naphthoquinone + NAD(P)H
2-methyl-1,4-naphthoquinol + NAD(P)+
-
artificial acceptor, trivial name menadione
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
additional information
?
-
-
lack of NQO1 in male mice increases benzene-induced hematotoxicity but not genotoxicity or the DNA damage response. NQO1 appears critical in female mice for detoxifying the metabolites of benzene responsible for genotoxicity, hematotoxicity, and induction of the DNA damage response
-
-
?
additional information
?
-
-
V5+ down-regulates Nqo1 at the transcriptional level, possibly through inhibiting the ATP-dependent activation of Nrf2
-
-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
lack of NQO1 in male mice increases benzene-induced hematotoxicity but not genotoxicity or the DNA damage response. NQO1 appears critical in female mice for detoxifying the metabolites of benzene responsible for genotoxicity, hematotoxicity, and induction of the DNA damage response
-
-
?
additional information
?
-
-
V5+ down-regulates Nqo1 at the transcriptional level, possibly through inhibiting the ATP-dependent activation of Nrf2
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
purified recombinant enzyme contains FAD whereas purified native enzyme does not contain FAD
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
As3+
-
induction of enzyme together with heme oxygenase-1 and glutathione S-transferase Ya
Cd2+
-
induction of enzyme together with heme oxygenase-1 and glutathione S-transferase Ya
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cr6+
-
decrease of enzyme mRNA level together with heme oxygenase-1 and glutathione S-transferase Ya
curcumin
-
inhibition of enzyme activity in vivo and in vitro. Inducues dissociation of complexes of enzyme with tumor suppressor protein p53 leading to degradation of p53, but not of p53 cancer hot-spot mutant R273H
ES936
-
pancreatic tumour xenografts in mice grow significantly slower following treatment with ES936
additional information
-
almond skin polyphenol extracted with agastrointestinal juice mimic decreases quinone reductase activity. Combining almond skin polyphenol extracted with agastrointestinal juice mimic plus vitamin C has an antagonistic effect
-
additional information
-
enzyme induction effects of series of methoxystilbenes (E and Z isomers) related to resveratrol on murine hepatoma cells, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,1'-(E)-ethene-1,2-diylbis(2-methoxybenzene)
-
at 12.5 micromol, induces quinone reductase to a greater extent than resveratrol
1,3-dimethoxy-2-[(E)-2-(4-methoxyphenyl)ethenyl]benzene
-
at 12.5 micromol, induces quinone reductase to a greater extent than resveratrol
1-methoxy-2-[(E)-2-(4-methoxyphenyl)ethenyl]benzene
-
at 6.3 micromol is 1.8 times more effective than resveratrol as a quinone reductase inducer
1-methoxy-3-[(E)-2-(4-methoxyphenyl)ethenyl]benzene
-
at 12.5 micromol, induces quinone reductase to a greater extent than resveratrol
2-methoxy-5-[(E)-2-(4-methoxyphenyl)ethenyl]phenol
-
at 12.5 micromol, induces quinone reductase to a greater extent than resveratrol
actinomycin D
-
treatment of the cells with actinomycin D alone for 6 h significantly inhibits the constitutive NQO1 mRNA level by approximately 80%. KTZ- and ITZ-mediated Nqo1 induction is completely inhibited
Clofibrate
-
administration to animals for 5 to 10 days, increase in enzyme protein and activity
itraconazole
-
induces NQO1 mRNA and enzymatic activity levels in a concentration- and time-dependent manner in wild-type but not aryl hydrocarbon receptor-deficient Hepa-1c1c7 cells. Increases NQO1 de novo RNA synthesis without significantly affecting the levels of existing RNA. 50 micromol shows maximum NQO1 mRNA induction
ketoconazole
-
induces NQO1 mRNA and enzymatic activity levels in a concentration- and time-dependent manner in wild-type but not aryl hydrocarbon receptor-deficient Hepa-1c1c7 cells. Increases NQO1 de novo RNA synthesis without significantly affecting the levels of existing RNA. 25 micromol shows maximum NQO1 mRNA induction
resveratrol
-
at 25 micromol increases quinone reductase activity by 1.5fold. Resveratrol induces quinone reductase activity of the wild type Hepa-1c1c7 cells to the same extent as the mutant c1 cells that lack a phase I enzyme
sulforaphane
-
at a concentration of 5 micromol significantly induces NQO1 mRNA in both wild-type and C12 cells
rutaecarpine
-
isolated from Evodia rutaecarpa, induces QR gene expression and activity through increase of activator protein-1, Evodia rutaecarpa is used in traditional Chinese medicine
rutaecarpine
-
induces enzyme activity and gene expression by transactivation of activator protein-1 in a dose-dependent manner
additional information
-
almond skin polyphenol extracted with methanol increases quinone reductase activity. Combining almond skin polyphenol extracted with methanol plus vitamin C results in a synergistic interaction
-
additional information
-
compared to resveratrol, analogues with ortho-methoxy substituents are more potent inducers of quinone reductase and exert their activity in a qualitatively different manner
-
additional information
-
heating at 42°C for 1 h significantly increases the expression of NQO1 in cancer cells
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.04
5-(1-aziridinyl)-3-(hydroxymethyl)-2-(3-hydroxy-1-propenyl)-1-methyl-1H-indole-4,7-dione
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.025
2,2'-dimethoxy-trans-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.025
2,4'-dimethoxy-trans-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.0081
2,4,4'-trimethoxy-cis-stilbene
Mus musculus
-
pH not specified in the publication, 37°C
0.025
2,4,4'-trimethoxy-trans-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.0103
2,6,4'-trimethoxy-trans-stilbene
Mus musculus
-
pH not specified in the publication, 37°C
0.025
2-hydroxy-4'-methoxy-trans-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.025
3,4'-dimethoxy-trans-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.0051
3,4,4'-trimethoxy-cis-stilbene
Mus musculus
-
pH not specified in the publication, 37°C
0.025
3,4,4'-trimethoxy-trans-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.000034
3,4,5,4'-tetramethoxy-cis-stilbene
Mus musculus
-
pH not specified in the publication, 37°C
0.001
3,4,5,4'-tetramethoxy-trans-stilbene
Mus musculus
-
pH not specified in the publication, 37°C
0.00059
3,5,4'-trimethoxy-cis-stilbene
Mus musculus
-
pH not specified in the publication, 37°C
0.0052
3,5,4'-trimethoxy-trans-stilbene
Mus musculus
-
pH not specified in the publication, 37°C
0.025
3,5-dihydroxy-4'-methoxy-cis-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.025
3,5-dihydroxy-4'-methoxy-trans-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.025
3-hydroxy-4'-methoxy-cis-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.025
3-hydroxy-4'-methoxy-trans-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.025
3-hydroxy-4,4'-dimethoxy-cis-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.025
3-hydroxy-4,4'-dimethoxy-trans-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.025
4,4'-dimethoxy-cis-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
0.025
4,4'-dimethoxy-trans-stilbene
Mus musculus
-
above, pH not specified in the publication, 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
leflunomide elicites significant induction of pulmonary CYP1A1 and NQO1 expression in neonatal mice
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
metabolism
-
NAD(P)H quinone oxidoreductase 1-mediated targeting of homocysteine-induced endoplasmic reticulum protein Herp to the proteasome is involved in Herp degradation. NQO1 is a target of nuclear factor E2-related factor Nrf2, which regulates cellular reactive oxygen speciesNrf2
physiological function
isoform NQO1-KO mice exhibit a marked increase of permeability and spontaneous inflammation in the gut. In the dextran sulfate sodium salt-induced colitis model, NQO1-KO mice show more severe inflammatory responses than NQO1-wild-type mice. The transcript levels of claudin and occludin, the major tight junction molecules of gut epithelial cells, are significantly decreased in NQO1-KO mice. The colons of NQO1-KO mice also show high levels of reactive oxygen species and histone deacetylase activity
physiological function
NQO1-null mice have greater lung tissue levels of D2- and E2-isoprostanes, the precursors of J2- and A2-isoprostanes, both at base line and following ozone exposure. A2-isoprostane inhibits ozone-induced NF-kappaB activation and IL-8 regulation
physiological function
treatment of the mouse melanoma cell line B16-BL6 with carnosic acid, a transcriptional inducer of the NQO1 gene, notably suppresses the cell killing effect of tyrosinase inhibitor rhododendrol. The effect is mostly abolished by NQO1 inhibitor ES936
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NQO1_MOUSE
274
0
30960
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
-
very unstable posttranslational modification is suggested that is not detectable by mass spectrometry
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion from a solution containing 10-15 mg/ml enzyme in 25 mM Tris-HCl, pH 8.0, 0.005 mM FAD, mixed with equal volumes of reservoir solution consisting of 30% polyethylene glycol 3350, 200 mM sodium acetate and 100 mM sodium tricine, pH 8.5, X-ray structure, 2.8 A resolution
hydrophilic isoform in the presence of FAD, hanging drop diffusion, 10 mg/ml enzyme, in 200 mM potassium phosphate, 0.5 mM EDTA, 0.5 mM, FAD, pH 8.0, 45-50% saturation of ammonium sulfate
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
after 48 h of exposure, 2,3-dehydrosilydianin at concentrations of 25 microM and higher significantly elevates the activity of NQO1 in murine hepatoma Hepa1c1c7 cells. 2,3-dehydrosilydianin causes the accumulation of Nrf2 and significantly induces the expression of the Nqo1 gene at both the mRNA and protein levels
in sub-chronic studies upon oral exposure to sulphoraphane for 30 days a 2- to 3fold increase in GSTM1, Gclc and NQO1 transcript levels, and a 2fold increase in NQO1 activity in adult livers is observed
leflunomide elicits significant induction of pulmonary CYP1A1 and NQO1 expression in neonatal mice. The dose at which leflunomide increases NQO1 is significantly higher than that required to induce CYP1A1 enzyme. Leflunomide also enhances hepatic CYP1A1, 1A2 and NQO1 expression in wild-type mice and fails to induce these enzymes in aryl hydrocarbon receptor-null mice
palm oil tocotrienol treatment increases NQO1 gene and protein expression in mice liver dose-dependently, with the highest expression seen in mice treated with 1000 mg/kg palm tocotrienol
sulforaphane or curcumin significantly increase NQO1 protein expression and activity without triggering G2/M cell cycle arrest or mitotic catastrophe. Sulforaphane and curcumin each increase the NQO1 activity within 24 h, at concentrations as low as 0.1 microM. The minimal quercetin concentration inducing NQO1, is 100fold higher than that which disrupts mitosis. Resveratrol modestly stimulates NQO1, but the minimally effective resveratrol concentration concomitantly induces evidence of cellular apoptosis
upon acute treatment with sulforaphane, increased GSTM1, NQO1, HO-1, and Gclc mRNA transcript levels are observed in adult liver, but no change in NQO1 activity
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
drug development
medicine
medicine
isoform NQO1-KO mice exhibit a marked increase of permeability and spontaneous inflammation in the gut. In the dextran sulfate sodium salt-induced colitis model, NQO1-KO mice show more severe inflammatory responses than NQO1-wild-type mice. The transcript levels of claudin and occludin, the major tight junction molecules of gut epithelial cells, are significantly decreased in NQO1-KO mice. The colons of NQO1-KO mice also show high levels of reactive oxygen species and histone deacetylase activity
medicine
in sub-chronic studies upon oral exposure to sulphoraphane for 30 days a 2- to 3fold increase in GSTM1, Gclc and NQO1 transcript levels, and a 2fold increase in NQO1 activity in adult livers is observed
drug development
-
ability of ketoconazole and itraconazole to induce NQO1 gene expression at the transcriptional level through an aryl hydrocarbon receptor-dependent mechanism
drug development
-
greater induction activities of the phase II enzyme quinone reductase associated with stilbenoids serve as a useful starting point for the design of improved chemopreventive agents
drug development
-
in vitro, almond skin polyphenols act as antioxidants and induce quinone reductase activity, but these actions are dependent upon their dose, method of extraction, and interaction with antioxidant vitamins
drug development
-
mild temperature heat shock elevates the NQO1 expression in cancer cells, which in turn markedly increases the sensitivity of the cells to the bioreductive drug beta-lapachone in vitro and in vivo
medicine
-
ascorbic acid may potentiate the therapeutic efficacy of As3+ in treatment of acute promyelotic leukemia by enhancing the expression of enzyme together with heme oxygenase-1 and glutathione S-transferase Ya
medicine
-
clofibrate-mediated hepatoprotection against acetaminophen does not appear to be dependent upon enhanced expression of enzyme. Conditions of 94% inhobition of enzyme do not increase the susceptibility of hepatocytes from clofibrate treated mice to acetaminophen
medicine
-
main function of QR1 is probably the detoxification of dietary quinones but it may also contribute to the reduction of vitamin K for its involvement in blood coagluation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Prochaska, H.J.; Talalay, P.
Purification and characterization of two isofunctional forms of NAD(P)H: quinone reductase from mouse liver
J. Biol. Chem.
261
1372-1378
1986
Mus musculus
Amzel, L.M.; Bryant, S.H.; Prochaska, H.J.; Talalay, P.
Preliminary crystallographic X-ray data for an NAD(P)H:quinone reductase from mouse liver
J. Biol. Chem.
261
1379
1986
Mus musculus
Chen, S.; Clarke, P.E.; Martino, P.A.; Deng, P.S.K.; Yeh, C.H.; Lee, T.D.; Prochaska, H.J.; Talalay, P.
Mouse liver NAD(P)H:quinone acceptor oxidoreductase: protein sequence analysis by tandem mass spectrometry, cDNA cloning, expression in Escherichia coli, and enzyme activity analysis
Protein Sci.
3
1296-1304
1994
Homo sapiens, Mus musculus, Rattus norvegicus
Chen, S.; Knox, R.; Lewis, A.D.; Friedlos, F.; Workman, P.; Deng, P.S.K.; Fung, M.; Ebenstein, D.; Wu, K.; Tsai, T.M.
Catalytic properties of NAD(P)H:quinone acceptor oxidoreductase: study involving mouse, rat, human, and mouse-rat chimeric enzymes
Mol. Pharmacol.
47
934-939
1995
Homo sapiens, Mus musculus, Rattus norvegicus
Faig, M.; Bianchet, M.A.; Talalay, P.; Chen, S.; Winski, S.; Ross, D.; Amzel, L.M.
Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release
Proc. Natl. Acad. Sci. USA
97
3177-3182
2000
Homo sapiens (P15559), Homo sapiens, Mus musculus (Q64669), Mus musculus
Bauer, A.K.; Faiola, B.; Abernethy, D.J.; Marchan, R.; Pluta, L.J.; Wong, V.A.; Roberts, K.; Jaiswal, A.K.; Gonzalez, F.J.; Butterworth, B.E.; Borghoff, S.; Parkinson, H.; Everitt, J.; Recio, L.
Genetic susceptibility to benzene-induced toxicity: role of NADPH:quinone oxidoreductase-1
Cancer Res.
63
929-935
2003
Mus musculus
Gustafson, D.L.; Siegel, D.; Rastatter, J.C.; Merz, A.L.; Parpal, J.C.; Kepa, J.K.; Ross, D.; Long, M.E.
Kinetics of NAD(P)H:quinone oxidoreductase I (NQO1) inhibition by mitomycin C in vitro and in vivo
J. Pharmacol. Exp. Ther.
305
1079-1086
2003
Homo sapiens, Mus musculus, Rattus norvegicus
Elbekai, R.H.; Duke, J.; El-Kadi, A.O.
Ascorbic acid differentially modulates the induction of heme oxygenase-1, NAD(P)H:quinone oxidoreductase 1 and glutathione S-transferase Ya by As(3+), Cd(2+) and Cr(6+)
Cancer Lett.
246
54-62
2007
Mus musculus
Korashy, H.M.; El-Kadi, A.O.
Transcriptional regulation of the NAD(P)H:quinone oxidoreductase 1 and glutathione S-transferase ya genes by mercury, lead, and copper
Drug Metab. Dispos.
34
152-165
2006
Mus musculus
Tsvetkov, P.; Asher, G.; Reiss, V.; Shaul, Y.; Sachs, L.; Lotem, J.
Inhibition of NAD(P)H:quinone oxidoreductase 1 activity and induction of p53 degradation by the natural phenolic compound curcumin
Proc. Natl. Acad. Sci. USA
102
5535-5540
2005
Mus musculus
Moffit, J.S.; Aleksunes, L.M.; Kardas, M.J.; Slitt, A.L.; Klaassen, C.D.; Manautou, J.E.
Role of NAD(P)H:quinone oxidoreductase 1 in clofibrate-mediated hepatoprotection from acetaminophen
Toxicology
230
197-206
2007
Homo sapiens, Mus musculus, Mus musculus CD-1
Ahn, H.; Nam, J.W.; Seo, E.K.; Mar, W.
Induction of NAD(P)H:Quinone Reductase by Rutaecarpine Isolated from the Fruits of Evodia rutaecarpa in the Murine Hepatic Hepa-1c1c7 Cell Line
Planta Med.
74
1387-1390
2008
Mus musculus
Korashy, H.M.; Brocks, D.R.; El-Kadi, A.O.
Induction of the NAD(P)H:quinone oxidoreductase 1 by ketoconazole and itraconazole: a mechanism of cancer chemoprotection
Cancer Lett.
258
135-143
2007
Mus musculus
Zhang, W.; Go, M.L.
Quinone reductase induction activity of methoxylated analogues of resveratrol
Eur. J. Med. Chem.
42
841-850
2007
Mus musculus
Song, C.W.; Chae, J.J.; Choi, E.K.; Hwang, T.S.; Kim, C.; Lim, B.U.; Park, H.J.
Anti-cancer effect of bio-reductive drug beta-lapachon is enhanced by activating NQO1 with heat shock
Int. J. Hyperthermia
24
161-169
2008
Homo sapiens, Mus musculus, Mus musculus C3H
Chen, C.Y.; Blumberg, J.B.
In vitro activity of almond skin polyphenols for scavenging free radicals and inducing quinone reductase
J. Agric. Food Chem.
56
4427-4434
2008
Mus musculus
Colucci, M.A.; Moody, C.J.; Couch, G.D.
Natural and synthetic quinones and their reduction by the quinone reductase enzyme NQO1: from synthetic organic chemistry to compounds with anticancer potential
Org. Biomol. Chem.
6
637-656
2008
Mus musculus, Rattus norvegicus, Homo sapiens (P15559), Homo sapiens
Bianchet, M.A.; Erdemli, S.B.; Amzel, L.M.
Structure, function, and mechanism of cytosolic quinone reductases
Vitam. Horm.
78
63-84
2008
Homo sapiens, Mesocricetus auratus, Mus musculus, Rattus norvegicus
Bafana, A.; Chakrabarti, T.
Lateral gene transfer in phylogeny of azoreductase enzyme
Comput. Biol. Chem.
32
191-197
2008
Rattus norvegicus (P05982), Saccharomyces cerevisiae (Q07923), Mus musculus (Q64669), Cavia porcellus (Q8CHK7)
Anwar-Mohamed, A.; El-Kadi, A.O.
Down-regulation of the detoxifying enzyme NAD(P)H:quinone oxidoreductase 1 by vanadium in Hepa 1c1c7 cells
Toxicol. Appl. Pharmacol.
236
261-269
2009
Mus musculus
Zhang, W.; Go, M.L.
Methoxylation of resveratrol: effects on induction of NAD(P)H quinone-oxidoreductase 1 (NQO1) activity and growth inhibitory properties
Bioorg. Med. Chem. Lett.
21
1032-1035
2011
Homo sapiens, Mus musculus
Nam, S.T.; Hwang, J.H.; Kim, D.H.; Park, M.J.; Lee, I.H.; Nam, H.J.; Kang, J.K.; Kim, S.K.; Hwang, J.S.; Chung, H.K.; Shong, M.; Lee, C.H.; Kim, H.
Role of NADH: quinone oxidoreductase-1 in the tight junctions of colonic epithelial cells
BMB Rep.
47
494-499
2014
Mus musculus (Q64669)
Maeda, T.; Tanabe-Fujimura, C.; Fujita, Y.; Abe, C.; Nanakida, Y.; Zou, K.; Liu, J.; Liu, S.; Nakajima, T.; Komano, H.
NAD(P)H quinone oxidoreductase 1 inhibits the proteasomal degradation of homocysteine-induced endoplasmic reticulum protein
Biochem. Biophys. Res. Commun.
473
1276-1280
2016
Mus musculus
Shrestha, A.K.; Patel, A.; Menon, R.T.; Jiang, W.; Wang, L.; Moorthy, B.; Shivanna, B.
Leflunomide induces NAD(P)H quinone dehydrogenase 1 enzyme via the aryl hydrocarbon receptor in neonatal mice
Biochem. Biophys. Res. Commun.
485
195-200
2017
Mus musculus (Q64669)
Roubalova, L.; Dinkova-Kostova, A.T.; Biedermann, D.; K?en, V.; Ulrichova, J.; Vrba, J.
Flavonolignan 2,3-dehydrosilydianin activates Nrf2 and upregulates NAD(P)H quinone oxidoreductase 1 in Hepa1c1c7 cells
Fitoterapia
119
115-120
2017
Mus musculus (Q64669), Mus musculus
Atia, A.; Alrawaiq, N.; Abdullah, A.
Tocotrienol-rich palm oil extract induces NAD(P)H quinone oxidoreductase 1 (NQO1) expression in mice liver
J. Appl. Pharm. Sci.
6
127-134
2016
Mus musculus (Q64669)
-
Kummarapurugu, A.B.; Fischer, B.M.; Zheng, S.; Milne, G.L.; Ghio, A.J.; Potts-Kant, E.N.; Foster, W.M.; Soderblom, E.J.; Dubois, L.G.; Moseley, M.A.; Thompson, J.W.; Voynow, J.A.
NADPH quinone oxidoreductase 1 regulates host susceptibility to ozone via isoprostane generation
J. Biol. Chem.
288
4681-4691
2013
Mus musculus (Q64669)
Jackson, S.J.; Singletary, K.W.; Murphy, L.L.; Venema, R.C.; Young, A.J.
Phytonutrients differentially stimulate NAD(P)H quinone oxidoreductase, inhibit proliferation, and trigger mitotic catastrophe in Hepa1c1c7 cells
J. Med. Food
19
47-53
2016
Mus musculus (Q64669)
Okubo, A.; Yasuhira, S.; Shibazaki, M.; Takahashi, K.; Akasaka, T.; Masuda, T.; Maesawa, C.
NAD(P)H dehydrogenase, quinone 1 (NQO1), protects melanin-producing cells from cytotoxicity of rhododendrol
Pigment cell Melanoma Res.
29
309-316
2016
Homo sapiens (P15559), Homo sapiens, Mus musculus (Q64669), Mus musculus
Philbrook, N.A.; Winn, L.M.
Sub-chronic sulforaphane exposure in CD-1 pregnant mice enhances maternal NADPH quinone oxidoreductase 1 (NQO1) activity and mRNA expression of NQO1, glutathione S-transferase, and glutamate-cysteine ligase potential implications for fetal protection aga
Reprod. Toxicol.
43
30-37
2014
Mus musculus (Q64669)
EXTERNAL LINKS (specific for EC-Number 1.6.5.2)
Transporter Classification Database (TCDB): 2.A.37.1.2, 2.A.37.1.1
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