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(R,S)-camphorquinone + NADPH + H+
(R,S)-camphorquinone + NADP+
-
-
-
?
1,2-naphthoquinone + NADPH + H+
1,2-naphthoquinol + NADP+
1,4-benzoquinone + NADPH + H+
1,4-benzoquinol + NADP+
1,4-naphthoquinone + NADPH + H+
1,4-naphthoquinol + NADP+
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+
2,3-dimethoxy-5-methyl-1,4-benzoquinone + NADPH + H+
2,3-dimethoxy-5-methyl-1,4-benzoquinol + NADP+
-
-
-
-
?
2,6-dimethoxy-1,4-benzoquinone + NADPH + H+
2,6-dimethoxy-1,4-benzoquinol + NADP+
-
-
-
?
2-methyl-1,4-naphthoquinone + NADPH + H+
2-methyl-1,4-naphthoquinol + NADP+
2-methyl-5-hydroxy-1,4-naphthoquinone + NADPH + H+
2-methyl-5-hydroxy-1,4-naphthoquinol + NADP+
-
-
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH + H+
5-hydroxy-1,4-naphthoquinol + NADP+
5-hydroxy-2-methyl-1,4-naphthoquinone + NADPH + H+
5-hydroxy-2-methyl-1,4-naphthoquinol + NADP+
-
-
-
-
?
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenequinol + NADP+
acenaphthenequinone + NADPH + H+
acenaphthenequinol + NADP+
-
-
-
?
benzoquinone + NADPH
benzohydroquinone + NADP+
-
specific for NADPH
-
-
?
benzoquinone + NADPH + H+
benzoquinol + NADP+
dichlorophenolindophenol + NADPH + H+
? + NADP+
-
about 15% of the activity with menadione
-
-
?
menadione + NADPH + H+
? + NADP+
-
two-electron transfer mechanism from NADPH to quinone
-
-
?
menadione + NADPH + H+
menadiol + NADP+
methyl p-benzoquinone + NADPH + H+
methyl p-benzoquinol + NADP+
NADH + Fe(CN)63-
NAD+ + Fe(CN)63-
-
with NADH the actuvity is less than 10% of the activity with NADPH
-
-
?
NADH + H+ + 1,4-naphthoquinone
NAD+ + 1,4-naphthoquinol
-
with NADH the activity is about 15% of the activity with NADPH
-
-
?
NADH + H+ + acceptor
NAD+ + reduced acceptor
-
no activity
-
-
?
NADH + H+ + coenzyme Q0
NAD+ + reduced coenzyme Q0
-
with NADH the activity is less than 10% of the activity with NADPH
-
-
?
NADH + H+ + coenzyme Q1
NAD+ + reduced coenzyme Q1
-
with NADH the activity is less than 10% of the activity with NADPH
-
-
?
NADH + H+ + dichlorophenolindophenol
NAD+ + reduced dichlorophenolindophenol
-
with NADH the actuvity is about 15% of the activity with NADPH
-
-
?
NADH + menadione
NAD+ + ?
-
with NADH the activity is less than 10% of the activity with NADPH
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
NADPH + H+ + 1,2-naphthoquinone-4-sulfonate
NADP+ + ?
NADPH + H+ + 1,4-benzoquinone
NADP+ + 1,4-benzohydroquinol
no activity with NADH
-
-
?
NADPH + H+ + 1,4-benzoquinone
NADP+ + ?
NADPH + H+ + 1,4-naphthoquinone
NADP+ + 1,4-naphthohydroquinone
-
-
-
?
NADPH + H+ + 1,4-naphthoquinone
NADP+ + 1,4-naphthoquinol
-
-
-
-
?
NADPH + H+ + 2,3-dichloro-5,6-dicyano-1,4-benzoquinone
NADP+ + 2,3-dichloro-5,6-dicyano-1,4-benzoquinol
-
-
-
?
NADPH + H+ + 2,5-dimethyl-4-benzoquinone
NADP+ + 2,5-dimethyl-4-benzoquinonl
-
-
-
-
?
NADPH + H+ + 2-hydroxy-1,4-naphthoquinone
NADP+ + 2-hydroxy-1,4-naphthoquinol
-
-
-
-
?
NADPH + H+ + 2-hydroxy-1,4-naphthoquinone
NADP+ + ?
NADPH + H+ + a quinone
NADP+ + a quinol
NADPH + H+ + anthraquinone-2-sulfonate
NADP+ + ?
-
-
-
-
?
NADPH + H+ + anthraquinone-2-sulfonic acid
NADP+ + ?
-
-
-
-
?
NADPH + H+ + catechol
NADP+ + ?
-
i.e. 1,2-dihydroxybenzene
-
-
?
NADPH + H+ + coenzyme Q0
NADP+ + reduced coenzyme Q0
-
-
-
-
?
NADPH + H+ + coenzyme Q1
NADP+ + reduced coenzyme Q1
-
-
-
-
?
NADPH + H+ + coenzyme Q10
NADP+ + reduced coenzyme Q10
-
-
-
-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
-
-
-
-
?
NADPH + H+ + dibromothymoquinone
NADP+ + dibromothymoquinol
-
-
-
-
?
NADPH + H+ + dichlorophenolindophenol
NADP+ + reduced dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + duroquinone
NADP+ + duroquinol
NADPH + H+ + menadione
NADP+ + ?
-
-
-
-
?
NADPH + H+ + menadione
NADP+ + menadiol
NADPH + H+ + menadione
NADP+ + reduced menadiol
-
-
-
-
?
NADPH + H+ + methyl-p-benzoquinone
NADP+ + methyl-p-benzohydroquinone
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + p-benzoquinone
NADP+ + p-benzohydroquinone
-
-
-
?
NADPH + H+ + phenyl-1,4-benzoquinone
NADP+ + phenyl-1,4-benzoquinol
-
-
-
?
NADPH + H+ + quinone
NADP+ + ?
-
TNF alpha and LPS induce Nqo1 mRNA expression
-
-
?
NADPH + H+ + quinone
NADP+ + quinol
-
-
-
?
NADPH + H+ + ubiquinone-1
NADP+ + ubihydroquinone-1
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NAD(P)+
-
very low activity with NADH
-
-
?
oxidized dichlorophenolindophenol + NADPH + H+
reduced dicholorophenolindophenol + NADP+
-
-
-
-
?
phenyl 1,4-benzoquinone + NADPH + H+
phenyl 1,4-benzoquinol + NADP+
ubiquinone-0 + NADPH + H+
ubiquinol-0 + NADP+
-
two-electron transfer mechanism from NADPH to quinone
-
-
?
ubiquinone-1 + NADPH + H+
ubiquinol-1 + NADP+
-
two-electron transfer mechanism from NADPH to quinone
-
-
?
additional information
?
-
1,2-naphthoquinone + NADPH + H+
1,2-naphthoquinol + NADP+
-
-
-
-
?
1,2-naphthoquinone + NADPH + H+
1,2-naphthoquinol + NADP+
-
-
-
-
?
1,4-benzoquinone + NADPH + H+
1,4-benzoquinol + NADP+
-
about 81% of the activity with menadione
-
-
?
1,4-benzoquinone + NADPH + H+
1,4-benzoquinol + NADP+
-
1,4-benzoquinone is oxidized almost stoichiometric amount of NADPH, suggesting that it is reduced to its hydroquinone with a two-electron reduction mechanism
-
-
?
1,4-benzoquinone + NADPH + H+
1,4-benzoquinol + NADP+
-
-
-
?
1,4-naphthoquinone + NADPH + H+
1,4-naphthoquinol + NADP+
-
about 85% of the activity with menadione
-
-
?
1,4-naphthoquinone + NADPH + H+
1,4-naphthoquinol + NADP+
-
two-electron transfer mechanism from NADPH to quinone
-
-
?
1,4-naphthoquinone + NADPH + H+
1,4-naphthoquinol + NADP+
-
1,4-naphthoquinone participates in the redox cycling in their reduction by this enzyme as evidenced by excess NADPH oxidation over quinone reduction. CBR4 may reduce 1,4-naphthoquinone in the two-electron reduction mechanism, but produces reactive superoxide and semiquinones through their redox cycling
-
-
?
1,4-naphthoquinone + NADPH + H+
1,4-naphthoquinol + NADP+
-
specific for NADPH
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
about 90% of the activity with menadione
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
-
?
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
-
-
-
-
?
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+
-
-
-
?
2 ferricyanide + NADPH + H+
2 ferrocyanide + NADP+
-
-
-
?
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+
-
i.e. menadione, specific for NADPH
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH + H+
5-hydroxy-1,4-naphthoquinol + NADP+
-
5-hydroxy-1,4-naphthoquinone participates in the redox cycling in their reduction by this enzyme as evidenced by excess NADPH oxidation over quinone reduction
-
-
?
5-hydroxy-1,4-naphthoquinone + NADPH + H+
5-hydroxy-1,4-naphthoquinol + NADP+
-
-
-
-
?
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenequinol + NADP+
-
9,10-phenanthrenequinone participates in the redox cycling in their reduction by this enzyme as evidenced by excess NADPH oxidation over quinone reduction. CBR4 may reduce 9,10-phenanthrenequinone in the two-electron reduction mechanism, but produces reactive superoxide and semiquinones through their redox cycling
-
-
?
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenequinol + NADP+
-
-
-
?
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenequinol + NADP+
-
-
-
-
?
benzoquinone + NADPH + H+
benzoquinol + NADP+
-
-
-
?
benzoquinone + NADPH + H+
benzoquinol + NADP+
-
-
-
?
menadione + NADPH + H+
menadiol + NADP+
-
reduction follows a two-electron-pathway
-
-
?
menadione + NADPH + H+
menadiol + NADP+
-
-
-
-
?
menadione + NADPH + H+
menadiol + NADP+
-
-
-
-
?
methyl p-benzoquinone + NADPH + H+
methyl p-benzoquinol + NADP+
-
-
-
?
methyl p-benzoquinone + NADPH + H+
methyl p-benzoquinol + NADP+
-
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
acceptor: ferricyanide
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
acceptor: menadione
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
acceptor: benzoquinone
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
acceptor: ferric chloride
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
acceptor: methylene blue
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
acceptor: FMN
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
aceptor: 1,10-phenanthroline
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
2,3',6-trichlorophenolindophenol is reduced to leuco-2,3',6-trichlorophenolindophenol
-
-
?
NADPH + H+ + 1,2-naphthoquinone-4-sulfonate
NADP+ + ?
-
i.e. Lawsone
-
-
?
NADPH + H+ + 1,2-naphthoquinone-4-sulfonate
NADP+ + ?
-
i.e. Lawsone
-
-
?
NADPH + H+ + 1,4-benzoquinone
NADP+ + ?
-
-
-
-
?
NADPH + H+ + 1,4-benzoquinone
NADP+ + ?
-
-
-
-
?
NADPH + H+ + 2-hydroxy-1,4-naphthoquinone
NADP+ + ?
-
-
-
-
?
NADPH + H+ + 2-hydroxy-1,4-naphthoquinone
NADP+ + ?
-
-
-
-
?
NADPH + H+ + a quinone
NADP+ + a quinol
-
-
-
-
?
NADPH + H+ + a quinone
NADP+ + a quinol
-
-
-
-
?
NADPH + H+ + a quinone
NADP+ + a quinol
-
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+ + duroquinone
NADP+ + duroquinol
-
-
-
-
?
NADPH + H+ + duroquinone
NADP+ + duroquinol
-
-
-
?
NADPH + H+ + duroquinone
NADP+ + duroquinol
-
-
-
-
?
NADPH + H+ + menadione
NADP+ + menadiol
-
-
-
?
NADPH + H+ + menadione
NADP+ + menadiol
-
-
-
-
?
phenyl 1,4-benzoquinone + NADPH + H+
phenyl 1,4-benzoquinol + NADP+
-
-
-
?
phenyl 1,4-benzoquinone + NADPH + H+
phenyl 1,4-benzoquinol + NADP+
-
-
-
?
additional information
?
-
-
the enzyme plays an important role in managing oxidative stress and contributes to successful colonization of the host
-
-
?
additional information
?
-
-
the enzyme exhibits NADPH-dependent reductase activity for o- and p-quinones, but not for other aldehydes and ketones. In vitro quinone reduction by CBR4 generates superoxide through the redox cycling, and suggest that the enzyme may be involved in the induction of apoptosis by cytotoxic 9,10-phenanthrenequinone
-
-
?
additional information
?
-
PA1225 does not react with methyl red and does not possess azoreductase activity and displays a negligible NADPH:O2 oxidase activity
-
-
-
additional information
?
-
-
PA1225 does not react with methyl red and does not possess azoreductase activity and displays a negligible NADPH:O2 oxidase activity
-
-
-
additional information
?
-
-
the bifunctional enzyme also shows activity with azo dyes and NAD(P)H as cofactor, cf. EC 1.7.1.6
-
-
?
additional information
?
-
-
the bifunctional enzyme also shows activity with azo dyes and NAD(P)H as cofactor, cf. EC 1.7.1.6
-
-
?
additional information
?
-
enzyme displays bifunctional 3alpha-hydroxysteroid dehydrogenase and NADPH reductase (quinone) activities. Quinone reduction occurs via a mechanism that differs from 3-ketosteroid reduction. In this mechanism, the electron donor NADPH and acceptor o-quinone are bound in close proximity, which permits hydride transfer without formal protonation of the acceptor carbonyl by Tyr 55
-
-
?
additional information
?
-
-
trace activity with substrates acrolein, cinnamaldehyde, 3-buten-2-one, 3-penten-2-one, 3-nonen-2-one
-
-
?
additional information
?
-
-
NADH, deazariboflavin, and methylviologen can also act as electron donors
-
-
?
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P187S
-
Pro187Ser polymorphism in NQO1 has a limited role in the development of Tardive dyskinesia (a potentially irreversible side effect of antipsychotic medication treatment that occurs in approximately 25% of chronically treated schizophrenia patients)
Q192R
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 60 min) relative to parental mutant variant B1G6
Q192R/A46P/V159A
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 90 min) relative to parental mutant variant 16B7
Q192R/A46P/V159A/A48P
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 60°C, 45 min) relative to parental mutant variant 2A1
Q192R/A46P/V159A/C129S
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 60°C, 45 min) relative to parental mutant variant 23C10
Q192R/A46P/V159A/C129S/A178D/A31S/K74E/A88G/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 2F11
Q192R/A46P/V159A/C129S/A178D/A77T/F98L/N131D
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 3B9
Q192R/A46P/V159A/C129S/A178D/A88G/N131D/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 1B6
Q192R/A46P/V159A/C129S/A178D/K74E/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 2E4
Q192R/A46P/V159A/C129S/A178D/N131D/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 85°C, 150 min) relative to parental mutant variant 6F11
Q192R/A46P/V159A/C129S/A77T/N131D
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 14D4
Q192R/A46P/V159A/C129S/D7H/A178D
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 13G10
Q192R/A46P/V159A/C129S/E36D/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 1C11
Q192R/A46P/V159A/C129S/I6V/T79R/Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 32F5
Q192R/A46P/V159A/C129S/K74E/A88G
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 23C5
Q192R/A46P/V159A/C129S/L161M/L169P
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 27E4
Q192R/A46P/V159A/C129S/N14D/L143Q
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 6F10
Q192R/A46P/V159A/C129S/Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 80°C, 60 min) relative to parental mutant variant 23E4
Q192R/A46P/V159A/Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 60°C, 45 min) relative to parental mutant variant 19E4
Q192R/Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 90 min) relative to parental mutant variant 12B8
Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 60 min) relative to parental mutant variant K7E3
Q192R
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 60 min) relative to parental mutant variant B1G6
-
Q192R/A46P/V159A
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 90 min) relative to parental mutant variant 16B7
-
Q192R/Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 90 min) relative to parental mutant variant 12B8
-
Y179H
-
site-directed mutagenesis, analysis of initial activity and thermostability (at 55°C, 60 min) relative to parental mutant variant K7E3
-
D50N
less than 0.1% of wild-type activity
H117A
less than 0.1% of wild-type activity
K84M
complete loss of activity
K84R
complete loss of activity
Y55F
narrow substrate specificity, reduction of selected aromatic quinones and alpha-dicarbonyls. The activation energy for 9,10-phenanthrenequinone reduction is unchanged in Y55 mutants
Y55S
narrow substrate specificity, reduction of selected aromatic quinones and alpha-dicarbonyls. The activation energy for 9,10-phenanthrenequinone reduction is unchanged in Y55 mutants
additional information
-
improvement of the kinetic and thermodynamic stability of the azoreductase by directed evolution via rational design approaches, five rounds of mutagenesis/recombination are followed by high-throughput screening. Mutant 1B6 shows a 300fold higher half-life at 50°C compared to the wild-type enzyme. mutant 1B6 has a folded state slightly less stable than the wild-type (with lower melting and optimal temperatures) but in contrast is more resistant to irreversible denaturation. The superior kinetic stability of 1B6 variant is therefore related to an increased resistance of the unfolded monomers to aggregation through the introduction of mutations that disturb hydrophobic patches and increase the surface net charge of the protein. Mutants 2A1 and 2A1-Y179H show increased thermodynamic stability with a 10-20°C higher melting temperature than wild-type, these residues are mostly involved in strengthening the solvent-exposed loops or the inter-dimer interactions of the folded state. Molecular details of mutations that improve stability, overview
additional information
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improvement of the kinetic and thermodynamic stability of the azoreductase by directed evolution via rational design approaches, five rounds of mutagenesis/recombination are followed by high-throughput screening. Mutant 1B6 shows a 300fold higher half-life at 50°C compared to the wild-type enzyme. mutant 1B6 has a folded state slightly less stable than the wild-type (with lower melting and optimal temperatures) but in contrast is more resistant to irreversible denaturation. The superior kinetic stability of 1B6 variant is therefore related to an increased resistance of the unfolded monomers to aggregation through the introduction of mutations that disturb hydrophobic patches and increase the surface net charge of the protein. Mutants 2A1 and 2A1-Y179H show increased thermodynamic stability with a 10-20°C higher melting temperature than wild-type, these residues are mostly involved in strengthening the solvent-exposed loops or the inter-dimer interactions of the folded state. Molecular details of mutations that improve stability, overview
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Jagendorf, A.T.
Chloroplast TPNH diaphorase
Methods Enzymol.
6
430-434
1963
Spinacia oleracea
-
brenda
Koli, A.K.; Yearby, C.; Scott, W.; Donaldson, K.O.
Purification and properties of three separate menadione reductases from hog liver
J. Biol. Chem.
244
621-629
1969
Sus scrofa
brenda
Pupillo, P.; de Luca, L.
Pyridine nucleotide-linked dehydrogenases (quinone dependent) in plasma membrane and endoplasmatic reticulum of plant cells
Dev. Plant Biol.
7
321-328
1982
Cucurbita pepo, Zea mays
-
brenda
Batot, G.; Martel, C.; Capdeville, N.; Wientjes, F.; Morel, F.
Characterization of neutrophil NADPH oxidase activity reconstituted in a cell-free assay using specific monoclonal antibodies raised against cytochrome b558
Eur. J. Biochem.
234
208-215
1995
Homo sapiens
brenda
Diatchuk, V.; Lotan, O.; Koshkin, V.; Wikstroem, P.; Pick, E.
Inhibition of NADPH oxidase activation by 4-(2-aminoethyl)-benzenesulfonyl fluoride and related compounds
J. Biol. Chem.
272
13292-13301
1997
Cavia porcellus, Homo sapiens
brenda
Viljoen, C.C.; Cloete, F.; Scott, W.E.
Isolation and characterization of an NAD(P)H dehydrogenase from the cyanobacterium, Microcystis aeruginosa
Biochim. Biophys. Acta
827
247-259
1985
Microcystis aeruginosa
-
brenda
Kim, W.H.; Chung, J.H.; Back, J.H.; Choi, J.; Cha, J.H.; Koh, H.Y.; Han, Y.S.
Molecular cloning and characterization of an NADPH quinone oxidoreductase from Kluyveromyces marxianus
J. Biochem. Mol. Biol.
36
442-449
2003
Kluyveromyces marxianus (Q8NJJ9), Kluyveromyces marxianus
brenda
Wang, G.; Maier, R.J.
An NADPH quinone reductase of Helicobacter pylori plays an important role in oxidative stress resistance and host colonization
Infect. Immun.
72
1391-1396
2004
Helicobacter pylori
brenda
Kitzing, K.; Fitzpatrick, T.B.; Wilken, C.; Sawa, J.; Bourenkov, G.P.; Macheroux, P.; Clausen, T.
The 1.3 A crystal structure of the flavoprotein YqjM reveals a novel class of Old Yellow Enzymes
J. Biol. Chem.
280
27904-27913
2005
Bacillus subtilis
brenda
Gharavi, N.; El-Kadi, A.O.
Role of nitric oxide in downregulation of cytochrome P450 1a1 and NADPH: Quinone oxidoreductase 1 by tumor necrosis factor-alpha and lipopolysaccharide
J. Pharm. Sci.
96
2795-2807
2007
Mus musculus
brenda
Hong, Y.; Wang, G.; Maier, R.J.
The NADPH quinone reductase MdaB confers oxidative stress resistance to Helicobacter hepaticus
Microb. Pathog.
44
169-174
2008
Helicobacter hepaticus, Helicobacter hepaticus ATCC 51449
brenda
Huang, S.K.; Chiu, A.W.; Pu, Y.S.; Huang, Y.K.; Chung, C.J.; Tsai, H.J.; Yang, M.H.; Chen, C.J.; Hsueh, Y.M.
Arsenic methylation capability, heme oxygenase-1 and NADPH quinone oxidoreductase-1 genetic polymorphisms and the stage and grade of urothelial carcinomas
Urol. Int.
80
405-412
2008
Homo sapiens
brenda
Wagner, A.E.; Hug, H.; Goessl, R.; Riss, G.; Mussler, B.; Elste, V.; Rimbach, G.; Barella, L.
The natural compound ascorbigen modulates NADPH-quinone oxidoreductase (NQO1) mRNA and enzyme activity levels in cultured liver cells and in laboratory rats
Ann. Nutr. Metab.
53
122-128
2008
Rattus norvegicus
brenda
Endo, S.; Matsunaga, T.; Kitade, Y.; Ohno, S.; Tajima, K.; El-Kabbani, O.; Hara, A.
Human carbonyl reductase 4 is a mitochondrial NADPH-dependent quinone reductase
Biochem. Biophys. Res. Commun.
377
1326-1330
2008
Homo sapiens
brenda
Lambertucci, R.H.; Hirabara, S.M.; Silveira, L.d.o.s..R.; Levada-Pires, A.C.; Curi, R.; Pithon-Curi, T.C.
Palmitate increases superoxide production through mitochondrial electron transport chain and NADPH oxidase activity in skeletal muscle cells
J. Cell. Physiol.
216
796-804
2008
Rattus norvegicus
brenda
Laurindo, F.R.; Fernandes, D.C.; Santos, C.X.
Assessment of superoxide production and NADPH oxidase activity by HPLC analysis of dihydroethidium oxidation products
Methods Enzymol.
441
237-260
2008
Homo sapiens
brenda
Zai, C.C.; Tiwari, A.K.; Basile, V.; de Luca, V.; Mueller, D.J.; Voineskos, A.N.; Remington, G.; Meltzer, H.Y.; Lieberman, J.A.; Potkin, S.G.; Kennedy, J.L.
Oxidative stress in tardive dyskinesia: Genetic association study and meta-analysis of NADPH quinine oxidoreductase 1 (NQO1) and superoxide dismutase 2 (SOD2, MnSOD) genes
Prog. Neuropsychopharmacol. Biol. Psychiatry
34
50-56
2009
Homo sapiens
brenda
Schlegel, B.P.; Ratnam, K.; Penning, T.M.
Retention of NADPH-linked quinone reductase activity in an aldo-keto reductase following mutation of the catalytic tyrosine
Biochemistry
37
11003-11011
1998
Rattus norvegicus (P23457)
brenda
Hayashi, M.; Ohzeki, H.; Shimada, H.; Unemoto, T.
NADPH-specific quinone reductase is induced by 2-methylene-4-butyrolactone in Escherichia coli
Biochim. Biophys. Acta
1273
165-170
1996
Escherichia coli
brenda
Crosas, E.; Porte, S.; Moeini, A.; Farres, J.; Biosca, J.A.; Pares, X.; Fernandez, M.R.
Novel alkenal/one reductase activity of yeast NADPH:quinone reductase Zta1p. Prospect of the functional role for the zeta-crystallin family
Chem. Biol. Interact.
191
32-37
2011
Saccharomyces cerevisiae
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
Brissos, V.; Goncalves, N.; Melo, E.; Martins, L.
Improving kinetic or thermodynamic stability of an azoreductase by directed evolution
PLoS ONE
9
e87209
2014
Pseudomonas putida, Pseudomonas putida MET94
brenda
Flores, E.; Gadda, G.
Kinetic characterization of PA1225 from Pseudomonas aeruginosa PAO1 reveals a new NADPH quinone reductase
Biochemistry
57
3050-3058
2018
Pseudomonas aeruginosa (Q9I4B3), Pseudomonas aeruginosa
brenda
Barcarolo, M.; Garavaglia, B.; Gottig, N.; Ceccarelli, E.; Catalano-Dupuy, D.; Ottado, J.
A novel Xanthomonas citri subsp. citri NADPH quinone reductase involved in salt stress response and virulence
Biochim. Biophys. Acta
1864
129514
2020
Xanthomonas citri (Q8PKE6), Xanthomonas citri 306 (Q8PKE6)
brenda