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1.6.5.5: NADPH:quinone reductase

This is an abbreviated version!
For detailed information about NADPH:quinone reductase, go to the full flat file.

Word Map on EC 1.6.5.5

Reaction

NADPH
+
H+
 + 2 quinone =
NADP+
 + 2 semiquinone

Synonyms

ArsH, Dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate) (quinone), DT-diaphorase, EC 1.6.99.2, Flavoprotein NAD(P)H:quinone reductase, Menadione oxidoreductase, Menadione reductase, NAD(P)H dehydrogenase, NAD(P)H dehydrogenase (quinone), NAD(P)H menadione reductase, NAD(P)H quinone reductase, NAD(P)H-quinone dehydrogenase, NAD(P)H-quinone oxidoreductase, NAD(P)H-quinone reductase, NAD(P)H:(quinone-acceptor) oxidoreductase, NAD(P)H:menadione oxidoreductase, NAD(P)H:paraquat diaphorase, NAD(P)H:quinone reductase, NADH-menadione reductase, NADH-menaquinone reductase, NADH:quinone reductase, NADPH DT-diaphorase, NADPH quinone acceptor oxidoreductase, NADPH-dependent quinone reductase, NADPH:azodicarbonyl/quinone reductase, NADPH:quinone oxidoreductase, NADPH:quinone reductase, Naphthoquinone reductase, NfsA, nitroreductase A, old yellow enzyme, ORF 17150, p-Benzoquinone reductase, P1-ZCr, P1-zeta-crystallin, P36, PA0660, Phylloquinone reductase, PtoQOR, QAO, Qor, QorA, Quinone reductase, Reduced NAD(P)H dehydrogenase, TcOYE, TmQR1, VAT-1, vesicle amine transport protein-1, Viologen accepting pyridine nucleotide oxidoreductase, Vitamin K reductase, ZCr, zeta-Crystallin, zeta-crystallin homolog protein, zeta-crystallin/NADPH:quinone oxidoreductase, zeta-Crystallin/quinone reductase, Zta1, Zta1p

ECTree

     1 Oxidoreductases
         1.6 Acting on NADH or NADPH
             1.6.5 With a quinone or similar compound as acceptor
                1.6.5.5 NADPH:quinone reductase

Crystallization

Crystallization on EC 1.6.5.5 - NADPH:quinone reductase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallographic structure of human zeta-crystallin is reported. Enzyme shows a tetrameric structure
structure in the free state at 2.3 A resolution. VAT-1 forms a dimer with the conserved NADPH-binding cleft on each protomer. The structure of VAT-1 in the NADP-bound state at 2.6 A resolution shows that NADP binds the binding cleft to create a putative active site with the nicotine ring
crystal structures of zeta-crystallin-like quinone oxidoreductase and its complexes with NADPH determined at 2.4 and 2.01 A resolution
-
native enzyme and its complex with NADPH at 2.3 A and 2.8 A resolution. QOR forms a homodimer in the crystal by interaction of the betaF-strands in domain II, forming a large beta-sheet that crosses the dimer interface. NADPH is located between the two domains in the QOR-NADPH complex. The disordered segment involved in the coenzyme binding of apo-QOR becomes ordered upon NADPH binding. The segment covers an NADPH-binding cleft and may serve as a lid. The 2'-phosphate group of the adenine of NADPH is surrounded by polar and positively charged residues in QOR, suggesting that QOR binds NADPH more readily than NADH. The putative substrate-binding site of QOR, is largely blocked by nearby residues