Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.6.5.2: NAD(P)H dehydrogenase (quinone)

This is an abbreviated version!
For detailed information about NAD(P)H dehydrogenase (quinone), go to the full flat file.

Word Map on EC 1.6.5.2

Reaction

NAD(P)H
+
H+
 +
a quinone
=
NAD(P)+
 +
a hydroquinone

Synonyms

1,4-benzoquinone reductase, azoreductase, chromate reductase, ChrR, dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate, quinone), diaphorase, DPND, DPNH-diaphorase, DT-diaphorase, DTD, DVU_2399, DVU_2400, DVU_2401, EC 1.6.99.2, FerB, ferric reductase B, flavoprotein NAD(P)H-quinone reductase, FlxABCD, FMN-dependent NAD(P)H:quinone oxidoreductase, Internal NADH dehydrogenase, MdaB, Menadione oxidoreductase, Menadione reductase, NAD(P)H dehydrogenase, NAD(P)H dehydrogenase complex, NAD(P)H menadione reductase, NAD(P)H quinone oxidoreductase, NAD(P)H quinone oxidoreductase-1, NAD(P)H quinone oxidoreductase1, NAD(P)H quinone reductase, NAD(P)H quinone-oxidoreductase 1, NAD(P)H-QR, NAD(P)H-quinone dehydrogenase, NAD(P)H-quinone oxidoreductase, NAD(P)H: (quinone acceptor) oxidoreductase, NAD(P)H: (quinone-acceptor)oxidoreductase, NAD(P)H: menadione oxidoreductase, NAD(P)H: Quinone oxidoreductase, NAD(P)H: quinone oxidoreductase 1, NAD(P)H: quinone oxidoreductase-1, NAD(P)H: quinone reductase, NAD(P)H:acceptor oxidoreductase, NAD(P)H:quinone acceptor oxidoreductase, NAD(P)H:quinone oxidoreducatase 1, NAD(P)H:quinone oxidoreductase, NAD(P)H:quinone oxidoreductase 1, NAD(P)H:quinone oxidoreductase I, NAD(P)H:quinone oxidoreductase-1, NAD(P)H:quinone reductase, NAD(P)H:quinoneoxidoreductase 1, NADH-menadione reductase, NADH:quinone oxidoreductase 1, NADPH quinone reductase, NADPH: quinone oxidoreductase-1, NADPH:quinone oxidoreductase, NADPH:quinone oxidoreductase 1, NAD[P]H:quinone acceptor oxidoreductase 1, Naphthoquinone reductase, Ndh complex, NDH2, nicotinamide adenine dinucleotide phosphate:quinone oxidoreductase 1, NQO1, NQR, NRH:quinone reductase 1, p-Benzoquinone reductase, Pden_4071, PfNdh2, Phylloquinone reductase, QOR2, QR1, QR2, Quinone reductase, quinone reductase 1, quinone reductase type 1, Reduced NAD(P)H dehydrogenase, reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase, TcpB, TmQR2, type II NADH: quinone oxidoreductase, Viologen accepting pyridine nucleotide oxidoreductase, Vitamin K reductase, vitamin-K reductase, WrbA

ECTree

     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.5 With a quinone or similar compound as acceptor
                1.6.5.2 NAD(P)H dehydrogenase (quinone)

Crystallization

Crystallization on EC 1.6.5.2 - NAD(P)H dehydrogenase (quinone)

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of WrbA with oxidized FMN
-
native enzyme and in complex with NADPH. The N-terminal domain, which adopts the Rossmann fold, provides a platform for NADPH binding, whereas the C-terminal domain, which contains a hydrophobic pocket connected to the NADPH-binding site, plays important roles in substrate binding. Asn143 near the NADPH-binding site is involved in substrate binding and catalysis
with and without FMN using the sitting drop vapor-diffusion technique
1H69 crystal structure-based in silico model of NQO1 active site, NQO1 complex with bound FAD and indolequinone
apo QR1 and QR1 in complex with duroquinone, to 2.0 A resolution
-
crystal structure of enzyme complexed with 5-methoxy-1,2-dimethyl-3-[(4-nitrophenoxy)methyl]indole-4,7-dione, 1.8 A resolution
dicumarol, RH1, E09 or ARH019 co-crystallized with NQO1
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, 1.7 A resolution
in complex with 4-hydroxy-6,7-dimethyl-3-(1-naphthylmethyl)-2H-chromen-2-one, hanging drop vapor diffusion method, using 2.4 M ammonium sulfate and 0.1 M Tris buffer pH 8.5
in complex with anticancer prodrug CB1954
-
in complex with inhibitor dicoumarol
mutant R139W, to 2.09 A resolution
structure of mutant P187S
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
-
purified recombinant wild-type andd selenomethionine-labeled His6-tagged wild-type enzyme in complex with NADH, X-ray diffraction structure determination and analysis at 1.4-1.75 A resolution, multiple wavelength anomalous dispersion using selenium anomalous signal, modeling
1.6 M ammonium sulfate, 150 mM imidazole, pH 7.0, small needles
-
hanging drop method, crystals from a solution of 10 mg/ml enzyme, 1.45 M ammonium sulfate, 0.5% polyethylene glycol 8000, 30 mM Cibacron blue and 150 mM imidazole, pH 7.0, complex with NADP+ or duroquinone, 2.1 A resolution, structure and substrate binding mechanism
-
QR1 in complex with NADP+ or QR1 in complex with duroquinone
-