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Information on EC 1.6.5.2 - NAD(P)H dehydrogenase (quinone) and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q07923

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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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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: Q07923
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
azoreductase
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dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone)
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diaphorase
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DT-diaphorase
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DTD
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flavoprotein NAD(P)H-quinone reductase
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FMN-dependent NAD(P)H:quinone oxidoreductase
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Menadione oxidoreductase
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Menadione reductase
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NAD(P)H dehydrogenase
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NAD(P)H menadione reductase
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NAD(P)H-quinone dehydrogenase
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NAD(P)H-quinone oxidoreductase
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NAD(P)H: (quinone-acceptor)oxidoreductase
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NAD(P)H: menadione oxidoreductase
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NADH-menadione reductase
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Naphthoquinone reductase
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p-Benzoquinone reductase
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Phylloquinone reductase
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QR1
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QR2
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Quinone reductase
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Reduced NAD(P)H dehydrogenase
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reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase
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Viologen accepting pyridine nucleotide oxidoreductase
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Vitamin K reductase
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vitamin-K reductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone
show the reaction diagram
ping-pong reaction mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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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 hide
9032-20-6
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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
NADH + H+ + a quinone
NAD+ + a hydroquinone
show the reaction diagram
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?
NADH + H+ + benzoquinone
NAD+ + benzoquinol
show the reaction diagram
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?
NADPH + H+ + a quinone
NADP+ + a hydroquinone
show the reaction diagram
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?
NADPH + H+ + benzoquinone
NADP+ + benzoquinol
show the reaction diagram
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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
NADH + H+ + a quinone
NAD+ + a hydroquinone
show the reaction diagram
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?
NADPH + H+ + a quinone
NADP+ + a hydroquinone
show the reaction diagram
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
benzoquinol
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shows noncompetitive inhibition in all conditions, it can bind to multiple enzyme forms or sites, even when either of the substrates (NADH or benzoquinone) is present at high concentrations
NAD+
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noncompetitive inhibition with either substrate when the other substrate is at low concentrations. At high NADH concentrations, NAD and benzoquinone are competitive, indicating they bind to a common site or sites
additional information
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the product inhibition pattern expected if WrbA follows a ping pong mechanism is that the pairs NAD/BQ and NADH/BQH2 display competitive inhibition, whereas the pairs NAD/NADH and BQ/BQH2 display non-competitive inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.9 - 36.3
benzoquinone
16.2 - 28.2
NADH
additional information
additional information
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WrbA steady-state kinetics, overview. Initial velocity as a function of either NADH or benzoquinone concentration present one or two Michaelis-Menten phases depends on the temperature at which the enzyme is held prior to assay. The effect of temperature is reversible, suggesting an intramolecular conformational process
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
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assay at room temperature
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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three subunits of the tetrameric enzyme contribute to each of four identical, cavernous active sites that appear to accommodate NAD(P)H or various quinones, but not simultaneously, suggesting an obligate tetramer with a ping-pong mechanism in which NAD departs before oxidized quinone binds
additional information
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dimer-tetramer assembly equilibrium documented for apoWrbA by analytical ultracentrifugation, large effect of temperature on the subunit assembly state of both apo- and holoWrbA, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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)
Manually annotated by BRENDA team
Murai, M.; Yamashita, T.; Senoh, M.; Mashimo, Y.; Kataoka, M.; Kosaka, H.; Matsuno-Yagi, A.; Yagi, T.; Miyoshi, H.
Characterization of the ubiquinone binding site in the alternative NADH-quinone oxidoreductase of Saccharomyces cerevisiae by photoaffinity labeling
Biochemistry
49
2973-2980
2010
Saccharomyces cerevisiae
Manually annotated by BRENDA team