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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)

Engineering

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

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N143A
residue near NADPH-binding site. About 10% of wild-type activity
N143L
residue near NADPH-binding site. About 10% of wild-type activity
W139A
residue near NADPH-binding site. About 30% of wild-type activity
W139F
residue near NADPH-binding site. Activity comparable to wild-type
W139I
residue near NADPH-binding site. About 50% of wild-type activity
Y140A
residue near NADPH-binding site. Almost complete loss of activity
Y140F
residue near NADPH-binding site. Activity comparable to wild-type
Y140I
residue near NADPH-binding site. Almost complete loss of activity
C609T
medicine
-
use of endogenous NQO1 enzyme for nanocarrier-based drug delivery in tumors. The rotaxane nanovalve system is composed of a linear stalk anchoring on the surface of mesoporous silica nanoparticles, an alpha-cyclodextrin ring that encircles it and locks the payload cargo molecules in the mesopores, and a benzoquinone stopper incorporated at the end of the stalk. The gate opening and controlled release of the cargo are triggered by cleavage of the benzoquinone stopper using an endogenous NQO1 enzyme
P187S
naturally occurring single-nucleotide polymorphism implicated in the development of various cancers. Crystal structure is almost identcal to wild-type, the amino acid exchange destabilizes interactions between the core and C-terminus, leading to depopulation of the native structure in solution and severely compromising the catalytic capacity of the variant protein
R139W
single nucleotide polymorphism, variant protein adopts the same structure both in the crystal as in solution, and kinetic parameters are similar to those reported for the wild-type protein. Thermostability of the variant is only slightly affected
E77A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
E77K
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
E77L
site-directed mutagenesis, almost inactive mutant
E77M
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
G115F
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
G115I
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
G118F
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
G118I
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
N18A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
N79A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
R13A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
R80E
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
R80K
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
R80L
site-directed mutagenesis, almost inactive mutant
R80M
site-directed mutagenesis, almost inactive mutant
R95E
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
S113A
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
S11A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
S16A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
Y46A
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
E77A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to wild-type
-
N18A
-
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
-
S11A
-
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
-
S16A
-
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
-
Y46A
-
site-directed mutagenesis, the mutation does not at all affect the enzyme activity
-
additional information