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Information on EC 1.6.5.10 - NADPH dehydrogenase (quinone) and Organism(s) Rattus norvegicus and UniProt Accession P23457

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IUBMB Comments
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 . Menaquinone can act as acceptor. The enzyme from hog liver is inhibited by dicoumarol and folic acid derivatives but not by 2,4-dinitrophenol .
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Rattus norvegicus
UNIPROT: P23457
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The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
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NADPH
+
H+
+
a quinone
=
NADP+
+
a quinol
+
+
=
+
Synonyms
nadph oxidase, nadph quinone oxidoreductase 1, nadph quinone oxidoreductase, nadph-quinone oxidoreductase, ppazor, xac2229, pa1225, nadph dehydrogenase (quinone), nadph:(quinone-acceptor) oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, reduced nicotinamide adenine dinucleotide phosphate (quinone)
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NADPH oxidase
NADPH-quinone oxidoreductase
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additional information
bifunctional 3alpha-hydroxysteroid dehydrogenase and NADPH reductase (quinone)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
37256-37-4
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(R,S)-camphorquinone + NADPH + H+
(R,S)-camphorquinone + NADP+
show the reaction diagram
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-
-
?
9,10-phenanthrenequinone + NADPH + H+
9,10-phenanthrenequinol + NADP+
show the reaction diagram
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-
-
?
acenaphthenequinone + NADPH + H+
acenaphthenequinol + NADP+
show the reaction diagram
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-
-
?
menadione + NADPH + H+
menadiol + NADP+
show the reaction diagram
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-
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-
?
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
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-
?
additional information
?
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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
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
NADPH + H+ + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
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-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cytochrome b558
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gp91phox and p22phox are integral membrane proteins that form a heterodimeric flavocytochrome b558, the catalytic core of the enzyme
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cytochrome c
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
diphenylene iodonium
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inhibition of the NADPH oxidase complex activity reduces the increase of superoxide production induced by palmitic acid
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
LITERATURE
IMAGE
0.002 - 0.056
9,10-phenanthrenequinone
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 2.85
9,10-phenanthrenequinone
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 1.43
9,10-phenanthrenequinone
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000003
substrate (R,S)-camphorquinone, mutant Y55F, pH 6.0, 25°C
0.00002
substrate (R,S)-camphorquinone, mutant Y55S, pH 6.0, 25°C
0.0006
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
0.0025
substrate (R,S)-camphorquinone, wild-type, pH 6.0, 25°C
0.0038
substrate acenaphthenequinone, wild-type, pH 6.0, 25°C
0.0044
substrate 9,10-phenanthrenenquinone, wild-type, pH 6.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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NQO1 activity is elevated (up to 20%) by ascorbigen treatment
Manually annotated by BRENDA team
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soleus, gastrocnemius, and quadriceps muscles, primary culture of cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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NADPH oxidase complex consists of membrane and cytosolic subunits
Manually annotated by BRENDA team
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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
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
DIDH_RAT
322
0
37028
Swiss-Prot
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team