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Enzyme Nomenclature
Information on EC 1.6.5.10 - NADPH dehydrogenase (quinone)
Word Map on EC 1.6.5.10
- 1.6.5.10
- superoxide
- neutrophil
- vascular
- p47phox
- endothelial
- phagocyte
- injury
- macrophage
- inflammation
- dysfunction
- apocynin
-
burst
- gp91phox
- artery
- dinucleotide
- hypertension
- leukocyte
- angiotensin
-
phorbol
- cardiovascular
- diabetes
- nicotinamide
- granulomatous
- iodonium
- monocyte
-
oxidases
-
diphenylene
- diphenyleneiodonium
- pma
- atherosclerosis
- myristate
-
mapks
-
polymorphonuclear
-
chemiluminescence
-
phagocytosis
-
ii-induced
- fmlp
-
endothelium-dependent
-
tempol
-
superoxide-generating
-
microbicidal
- myeloperoxidase
- peroxynitrite
-
phagosomes
- microglial
-
flavocytochrome
-
zymosan
- medicine
-
fmlp-induced
-
nadph-oxidase
-
ros-dependent
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Specify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
1.6.5.10
-
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RECOMMENDED NAME
GeneOntology No.
NADPH dehydrogenase (quinone)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
NADPH + H+ + a quinone = NADP+ + a quinol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
NADPH:(quinone-acceptor) oxidoreductase
A flavoprotein [1, 2]. The enzyme from Escherichia coli is specific for NADPH and is most active with quinone derivatives and ferricyanide as electron acceptors [3].
Menaquinone can act as acceptor. The enzyme from hog liver is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol [1].
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CAS REGISTRY NUMBER
COMMENTARY
37256-37-4
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme is a member of the family of NADPH-dependent FMN reductases
physiological function
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
physiological function
-
presence of Zta1p has an in vivo protective effect on yeast strains exposed to the toxic substrate 3-penten-2-one
physiological function
-
ArsH plays a role in the response to oxidative stress caused by arsenite
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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
(R,S)-camphorquinone + NADPH + H+
(R,S)-camphorquinone + NADP+
-
-
-
?
2,3-dimethoxy-5-methyl-1,4-benzoquinone + NADPH + H+
2,3-dimethoxy-5-methyl-1,4-benzoquinol + NADP+
-
-
-
-
?
2-methyl-5-hydroxy-1,4-naphthoquinone + NADPH + H+
2-methyl-5-hydroxy-1,4-naphthoquinol + NADP+
-
-
-
-
?
5-hydroxy-2-methyl-1,4-naphthoquinone + NADPH + H+
5-hydroxy-2-methyl-1,4-naphthoquinol + NADP+
-
-
-
-
?
benzoquinone + NADPH
benzohydroquinone + NADP+
-
specific for NADPH
-
-
?
dichlorophenolindophenol + NADPH + H+
? + NADP+
-
about 15% of the activity with menadione
-
-
?
menadione + NADPH + H+
? + NADP+
-
two-electron transfer mechanism from NADPH to quinone
-
-
?
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+ + 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 + H+ + 1,4-benzoquinone
NADP+ + 1,4-benzohydroquinol
no activity with NADH
-
-
?
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+ + 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+ + dichlorophenolindophenol
NADP+ + reduced dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + methyl-p-benzoquinone
NADP+ + methyl-p-benzohydroquinone
-
-
-
?
NADPH + H+ + oxidized 2,6-dichlorophenolindophenol
NADP+ + reduced 2,6-dichlorophenolindophenol
-
-
-
-
?
NADPH + H+ + phenyl-1,4-benzoquinone
NADP+ + phenyl-1,4-benzoquinol
-
-
-
?
NADPH + H+ + quinone
NADP+ + ?
-
TNF alpha and LPS induce Nqo1 mRNA expression
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NAD(P)+
-
very low activity with NADH
-
-
?
oxidized dichlorophenolindophenol + NADPH + H+
reduced dicholorophenolindophenol + 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
-
-
?
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-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-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+
-
-
-
-
?
menadione + NADPH + H+
menadiol + NADP+
-
reduction follows a two-electron-pathway
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
-
acceptor: ferric chloride
-
-
?
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
-
-
?
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
?
-
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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)
-
-
?
additional information
?
-
-
the enzyme plays an important role in managing oxidative stress and contributes to successful colonization of the host
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cytochrome b558
-
gp91phox and p22phox are integral membrane proteins that form a heterodimeric flavocytochrome b558, the catalytic core of the enzyme
-
FAD
-
enzyme displays flavin absorption spectrum with peaks at 376 and 456 nm and a shoulder at around 484 nm. Protein caontains FAD
flavin
-
flavoprotein, adsorption spectrum with a major peak at 456 nm
NADPH
-
NADH could also be used as an electron donor to MdaB but with much lower efficiency, about 3% of those with NADPH
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(N-methyl-4'-pyridyl) porphyrin
-
iron tetrakis, FeTMPyP, no inhibitory activity
Cibacron blue F3GA
-
the 1,4-naphthoquinone activity of CBR4 is potently inhibited, competitive with respect to NADPH
diphenylene iodonium
-
inhibition of the NADPH oxidase complex activity reduces the increase of superoxide production induced by palmitic acid
Procion red HE3B
-
the 1,4-naphthoquinone activity of CBR4 is potently inhibited, competitive with respect to NADPH
4-(2-aminoethyl)benzenesulfonylfluoride
-
0.206 mM, 50% inhibition, noncompetitive vs. NADPH, competitive vs. p47-phox in the concentration range of 0.5-2.0 mM
NADP+
-
the 1,4-naphthoquinone activity of CBR4 is potently inhibited, competitive with respect to NADPH
NADP+
-
NADP+ acts as a competitive inhibitor for NADPH binding at the active site of an enzyme
additional information
-
insensitive to 4-chloromercuribenzoate at 100 microM, heavy metals such as Cu2+, Co2+, Cd2+ and Mn2+ at 10 microM each, and chelating agents such as EDTA, o-phenanthroline and diethyldithiocarbamate at 100 microM each
-
additional information
-
the enzyme is insensitive to dicuomarol and quercetin, potent inhibitors of cytosolic quinone reductases
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
palmitic acid and antimycin A induce the enzyme and superoxide production
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0013
2,5-dimethyl-4-benzoquinone
-
pH 8.0, 25°C, recombinant His-tagged enzyme
0.0237
2-Hydroxy-1,4-naphthoquinone
-
pH 8.0, 25°C, recombinant His-tagged enzyme
0.0345
anthraquinone-2-sulfonate
-
pH 8.0, 25°C, recombinant His-tagged enzyme
additional information
additional information
-
stopped-flow and steady-state kinetics, overview
-
0.009
1,2-naphthoquinone
-
pH 7.0, temperature not specified in the publication
0.004
9,10-phenanthrenequinone
-
pH 7.0, temperature not specified in the publication
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
36.7
2,5-dimethyl-4-benzoquinone
Synechocystis sp.
-
pH 8.0, 25°C, recombinant His-tagged enzyme
11
2-Hydroxy-1,4-naphthoquinone
Synechocystis sp.
-
pH 8.0, 25°C, recombinant His-tagged enzyme
9.4
anthraquinone-2-sulfonate
Synechocystis sp.
-
pH 8.0, 25°C, recombinant His-tagged enzyme
4.2
1,2-naphthoquinone
Saccharomyces cerevisiae
-
pH 7.0, temperature not specified in the publication
1.45
9,10-phenanthrenequinone
Rattus norvegicus
P23457
mutant Y55F, pH 6.0, 25°C; mutant Y55S, pH 6.0, 25°C
4.2
9,10-phenanthrenequinone
Saccharomyces cerevisiae
-
pH 7.0, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
462
1,2-naphthoquinone
Saccharomyces cerevisiae
-
pH 7.0, temperature not specified in the publication
1907
1041
9,10-phenanthrenequinone
Saccharomyces cerevisiae
-
pH 7.0, temperature not specified in the publication
558
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008 - 0.01
dicoumarol
Synechocystis sp.
-
with dichlorophenolindophenol, pH 8.0, 25°C, recombinant His-tagged enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0006
substrate acenaphthenequinone, mutant Y55F, pH 6.0, 25°C; substrate acenaphthenequinone, mutant Y55S, pH 6.0, 25°C
0.0007
-
TNFalpha and LPS inhibit the beta-naphthoflavone induced increase in activity
0.0016
substrate 9,10-phenanthrenenquinone, mutant Y55S, pH 6.0, 25°C
0.0018
substrate 9,10-phenanthrenenquinone, mutant Y55F, pH 6.0, 25°C
1.097
-
activity of purified cytochrome b558 reconstituted with neutrophil membrane phospholipids, activation with arachidonic acid
1.258
-
activity of purified cytochrome b558 reconstituted with neutrophil membrane phospholipids, activation with sodiumdodecylsulfate
additional information
additional information
-
90300 units/mg, 1 unit is defined as that amount of enzyme causing an absorption change of 0.001 units/min at the specific wavelength
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the pH dependency of 9,10-phenanthrenequinone reduction catalyzed by the wild-type enzyme is different to that observed for 3-ketosteroid reduction. The kcat value for 9,10-phenanthrenequinone reduction is pH-dependent with the maximal rate decreasing with increasing pH but reveals an ionizable group with a pKb of 8.90 that must be protonated for maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
soleus, gastrocnemius, and quadriceps muscles, primary culture of cells
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
NADPH oxidase complex consists of membrane and cytosolic subunits
-
CBR4 is a mitochondrial matrix protein, its N-terminal signal is not cleaved
-
NADPH oxidase complex consists of membrane and cytosolic subunits. The gp91phox and p22phox are integral membrane proteins that form a heterodimeric flavocytochrome b558, the catalytic core of the enzyme
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42000
additional information
-
enzyme displays three charge isomers with different relative mobilities
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tetramer
additional information
-
NADPH oxidase complex consists of membrane and cytosolic subunits. The gp91phox and p22phox are integral membrane proteins that form a heterodimeric flavocytochrome b558, the catalytic core of the enzyme
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method. In addition to the oxidized and reduced enzyme form, the structures of the complexes with p-hydroxybenzaldehyde and p-nitrophenol, respectively are solved
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cytosolic components p67-phox and p47-phox of the multicomponent NADPH oxidase
-
gene arsh, expression as N-terminallyy His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
overexpression of CBR4 in bovine endothelial cells reveals that the enzyme has a non-cleavable mitochondrial targeting signal
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
induction under different types of cellular stress, including ethanol and dimethylsulfoxide exposure and by reaching the stationary growth phase
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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)
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
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Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
arsenic exposure is associated with an increased risk of urothelial carcinoma, inorganic arsenic, monomethylarsonic acid, and dimethylarsinic acid, are determined in urothelial carcinoma patients from arsenic-contaminated areas of southwestern Taiwan, no correlation of the arsenic methylation capability of the patients and C609T genotype of NQO1 is found
medicine
-
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)
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LINKS TO OTHER DATABASES (specific for EC-Number 1.6.5.10)
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