EzCatDB: S00343

DB codeS00343
CATH domainDomain 13.40.50.360Catalytic domain
E.C.1.6.5.2
CSA1d4a
MACiEM0003

CATH domainRelated DB codes (homologues)
3.40.50.360S00522,M00006,M00154

Enzyme Name
Swiss-protKEGG

P15559Q64669P05982
Protein nameNAD(P)H dehydrogenase [quinone] 1NAD(P)H dehydrogenase [quinone] 1NAD(P)H dehydrogenase [quinone] 1NAD(P)H dehydrogenase (quinone)
menadione reductase
phylloquinone reductase
quinone reductase
dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate,quinone)
DT-diaphorase
flavoprotein NAD(P)H-quinone reductase
menadione oxidoreductase
NAD(P)H dehydrogenase
NAD(P)H menadione reductase
NAD(P)H-quinone dehydrogenase
NAD(P)H-quinone oxidoreductase
NAD(P)H: (quinone-acceptor)oxidoreductase
NAD(P)H: menadione oxidoreductase
NADH-menadione reductase
naphthoquinone reductase
p-benzoquinone reductase
reduced NAD(P)H dehydrogenase
viologen accepting pyridine nucleotide oxidoreductase
vitamin K reductase
diaphorase
reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase
vitamin-K reductase
NAD(P)H2 dehydrogenase (quinone)
NQO1
QR1
NAD(P)H:(quinone-acceptor) oxidoreductase
SynonymsEC 1.6.5.2
Quinone reductase 1
NAD(P)H:quinone oxidoreductase 1
QR1
DT-diaphorase
DTD
Azoreductase
Phylloquinone reductase
Menadione reductase
EC 1.6.5.2
Quinone reductase 1
NAD(P)H:quinone oxidoreductase 1
QR1
DT-diaphorase
DTD
Azoreductase
Phylloquinone reductase
Menadione reductase
EC 1.6.5.2
Quinone reductase 1
NAD(P)H:quinone oxidoreductase 1
QR1
DT-diaphorase
DTD
Azoreductase
Phylloquinone reductase
Menadione reductase

KEGG pathways
MAP codePathways
MAP00100Biosynthesis of steroids

Swiss-prot:Accession NumberP15559Q64669P05982
Entry nameNQO1_HUMANNQO1_MOUSENQO1_RAT
ActivityNAD(P)H + a quinone = NAD(P)(+) + a hydroquinone.NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone.NAD(P)H + a quinone = NAD(P)(+) + a hydroquinone.
SubunitHomodimer.Homodimer (By similarity).Homodimer.
Subcellular locationCytoplasm.Cytoplasm.Cytoplasm.
CofactorFAD.FAD.FAD.


CofactorsSubstratesProducts
KEGG-idC00016C00038C00005C00004C00080C00472C00006C00003C00530
CompoundFADZincNADPHNADHH+QuinoneNADP+NAD+Hydroquinone
Typeamide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotideheavy metalamide group,amine group,nucleotideamide group,amine group,nucleotideothersaromatic ring (only carbon atom)amide group,amine group,nucleotideamide group,amine group,nucleotidearomatic ring (only carbon atom)
1d4aABound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1d4aBBound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1d4aCBound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1d4aDBound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1dxoABound:FADUnboundUnboundUnbound
Analogue:DQNUnboundUnboundUnbound
1dxoBBound:FADUnboundUnboundUnbound
Analogue:DQNUnboundUnboundUnbound
1dxoCBound:FADUnboundUnboundUnbound
Analogue:2xDQNUnboundUnboundUnbound
1dxoDBound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1dxqABound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1dxqBBound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1dxqCBound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1dxqDBound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1gg5ABound:FADUnboundUnboundUnbound
Analogue:E09UnboundUnboundUnbound
1gg5BBound:FADUnboundUnboundUnbound
Analogue:E09UnboundUnboundUnbound
1gg5CBound:FADUnboundUnboundUnbound
Analogue:E09UnboundUnboundUnbound
1gg5DBound:FADUnboundUnboundUnbound
Analogue:E09UnboundUnboundUnbound
1h66ABound:FADUnboundUnboundUnbound
Analogue:RH1UnboundUnboundUnbound
1h66BBound:FADUnboundUnboundUnbound
Analogue:RH1UnboundUnboundUnbound
1h66CBound:FADUnboundUnboundUnbound
Analogue:RH1UnboundUnboundUnbound
1h66DBound:FADUnboundUnboundUnbound
Analogue:RH1UnboundUnboundUnbound
1h69ABound:FADUnboundUnboundUnbound
Analogue:ARHUnboundUnboundUnbound
1h69BBound:FADUnboundUnboundUnbound
Analogue:ARHUnboundUnboundUnbound
1h69CBound:FADUnboundUnboundUnbound
Analogue:ARHUnboundUnboundUnbound
1h69DBound:FADUnboundUnboundUnbound
Analogue:ARHUnboundUnboundUnbound
1kboABound:FADUnboundUnboundUnbound
Analogue:340UnboundUnboundUnbound
1kboBBound:FADUnboundUnboundUnbound
Analogue:340UnboundUnboundUnbound
1kboCBound:FADUnboundUnboundUnbound
Analogue:340UnboundUnboundUnbound
1kboDBound:FADUnboundUnboundUnbound
Analogue:340UnboundUnboundUnbound
1kbqABound:FADUnboundUnboundUnbound
Analogue:936UnboundUnboundUnbound
1kbqBBound:FADUnboundUnboundUnbound
Analogue:936UnboundUnboundUnbound
1kbqCBound:FADUnboundUnboundUnbound
Analogue:936UnboundUnboundUnbound
1kbqDBound:FADUnboundUnboundUnbound
Analogue:936UnboundUnboundUnbound
1qbgABound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1qbgBBound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1qbgCBound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1qbgDBound:FADUnboundUnboundUnbound
UnboundUnboundUnboundUnbound
1qrdABound:FADUnboundUnboundUnbound
Analogue:DQNUnboundUnboundUnbound
1qrdBBound:FADUnboundUnboundUnbound
Analogue:DQNUnboundUnboundUnbound

Active-site residues
resource
PDB;1h66 & literature [3]
pdbCatalytic residues
1d4aAGLY 149;TYR 155;HIS 161
1d4aBGLY 149;TYR 155;HIS 161
1d4aCGLY 149;TYR 155;HIS 161
1d4aDGLY 149;TYR 155;HIS 161
1dxoAGLY 149;TYR 155;HIS 161
1dxoBGLY 149;TYR 155;HIS 161
1dxoCGLY 149;TYR 155;HIS 161
1dxoDGLY 149;TYR 155;HIS 161
1dxqAGLY 149;TYR 155;HIS 161
1dxqBGLY 149;TYR 155;HIS 161
1dxqCGLY 149;TYR 155;HIS 161
1dxqDGLY 149;TYR 155;HIS 161
1gg5AGLY 149;TYR 155;HIS 161
1gg5BGLY 149;TYR 155;HIS 161
1gg5CGLY 149;TYR 155;HIS 161
1gg5DGLY 149;TYR 155;HIS 161
1h66AGLY 149;TYR 155;HIS 161
1h66BGLY 149;TYR 155;HIS 161
1h66CGLY 149;TYR 155;HIS 161
1h66DGLY 149;TYR 155;HIS 161
1h69AGLY 149;TYR 155;HIS 161
1h69BGLY 149;TYR 155;HIS 161
1h69CGLY 149;TYR 155;HIS 161
1h69DGLY 149;TYR 155;HIS 161
1kboAGLY 149;TYR 155;HIS 161
1kboBGLY 149;TYR 155;HIS 161
1kboCGLY 149;TYR 155;HIS 161
1kboDGLY 149;TYR 155;HIS 161
1kbqAGLY 149;TYR 155;HIS 161
1kbqBGLY 149;TYR 155;HIS 161
1kbqCGLY 149;TYR 155;HIS 161
1kbqDGLY 149;TYR 155;HIS 161
1qbgAGLY 149;TYR 155;HIS 161
1qbgBGLY 149;TYR 155;HIS 161
1qbgCGLY 149;TYR 155;HIS 161
1qbgDGLY 149;TYR 155;HIS 161
1qrdAGLY 149;TYR 155;HIS 161
1qrdBGLY 149;TYR 155;HIS 161

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Fig.8, p.8849-8850
[6]p.612-614
[7]p.9985-9986
[10]p.278-279
[13]Fig.1, Fig.4, p.130-131
[14]p.244
[15]p.664-665
[19]Fig.8

references
[1]
PubMed ID1510975
JournalBiochemistry
Year1992
Volume31
Pages7879-85
AuthorsSiegel D, Beall H, Senekowitsch C, Kasai M, Arai H, Gibson NW, Ross D
TitleBioreductive activation of mitomycin C by DT-diaphorase.
[2]
PubMed ID7530954
JournalBiochem Pharmacol
Year1995
Volume49
Pages127-40
AuthorsCadenas E
TitleAntioxidant and prooxidant functions of DT-diaphorase in quinone metabolism.
[3]
CommentsX-ray crystallography
PubMed ID7568029
JournalProc Natl Acad Sci U S A
Year1995
Volume92
Pages8846-50
AuthorsLi R, Bianchet MA, Talalay P, Amzel LM
TitleThe three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction.
Related PDB1qrd
[4]
PubMed ID8999809
JournalJ Biol Chem
Year1997
Volume272
Pages1437-9
AuthorsChen S, Knox R, Wu K, Deng PS, Zhou D, Bianchet MA, Amzel LM
TitleMolecular basis of the catalytic differences among DT-diaphorase of human, rat, and mouse.
[5]
PubMed ID9050836
JournalProc Natl Acad Sci U S A
Year1997
Volume94
Pages1669-74
AuthorsZhao Q, Yang XL, Holtzclaw WD, Talalay P
TitleUnexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase).
[6]
PubMed ID10917652
JournalBiochem Soc Trans
Year1999
Volume27
Pages610-5
AuthorsBianchet MA, Foster C, Faig M, Talalay P, Amzel LM
TitleStructure and mechanism of cytosolic quinone reductases.
[7]
CommentsX-ray crystallography
PubMed ID10433694
JournalBiochemistry
Year1999
Volume38
Pages9881-6
AuthorsFoster CE, Bianchet MA, Talalay P, Zhao Q, Amzel LM
TitleCrystal structure of human quinone reductase type 2, a metalloflavoprotein.
Related PDB1qr2,2qr2
[8]
CommentsX-ray crystallography
PubMed ID10543876
JournalJ Med Chem
Year1999
Volume42
Pages4325-30
AuthorsSkelly JV, Sanderson MR, Suter DA, Baumann U, Read MA, Gregory DS, Bennett M, Hobbs SM, Neidle S
TitleCrystal structure of human DT-diaphorase: a model for interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954).
Related PDB1qbg
[9]
PubMed ID10419545
JournalMol Pharmacol
Year1999
Volume56
Pages272-8
AuthorsChen S, Wu K, Zhang D, Sherman M, Knox R, Yang CS
TitleMolecular characterization of binding of substrates and inhibitors to DT-diaphorase: combined approach involving site-directed mutagenesis, inhibitor-binding analysis, and computer modeling.
[10]
PubMed ID11035256
JournalFree Radic Biol Med
Year2000
Volume29
Pages276-84
AuthorsChen S, Wu K, Knox R
TitleStructure-function studies of DT-diaphorase (NQO1) and NRH: quinone oxidoreductase (NQO2).
[11]
PubMed ID10877993
JournalFront Biosci
Year2000
Volume5
PagesD639-48
AuthorsBeall HD, Winski SI
TitleMechanisms of action of quinone-containing alkylating agents. I: NQO1-directed drug development.
[12]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
Medline ID20202608
PubMed ID10706635
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages3177-82
AuthorsFaig M, Bianchet MA, Talalay P, Chen S, Winski S, Ross D, Amzel LM
TitleStructures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release.
Related PDB1d4a,1dxo,1dxq
Related Swiss-protP15559
[13]
PubMed ID10694883
JournalTrends Biochem Sci
Year2000
Volume25
Pages126-32
AuthorsFraaije MW, Mattevi A
TitleFlavoenzymes: diverse catalysts with recurrent features.
[14]
PubMed ID11035252
JournalFree Radic Biol Med
Year2000
Volume29
Pages241-5
AuthorsFoster CE, Bianchet MA, Talalay P, Faig M, Amzel LM
TitleStructures of mammalian cytosolic quinone reductases.
[15]
CommentsX-ray crystallography
PubMed ID11587640
JournalStructure (Camb)
Year2001
Volume9
Pages659-67
AuthorsFaig M, Bianchet MA, Winski S, Hargreaves R, Moody CJ, Hudnott AR, Ross D, Amzel LM
TitleStructure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones.
Related PDB1gg5,1h66,1h69
[16]
CommentsX-ray crystallography
PubMed ID11735396
JournalBiochemistry
Year2001
Volume40
Pages15135-42
AuthorsWinski SL, Faig M, Bianchet MA, Siegel D, Swann E, Fung K, Duncan MW, Moody CJ, Amzel LM, Ross D
TitleCharacterization of a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1 by biochemical, X-ray crystallographic, and mass spectrometric approaches.
Related PDB1kbo,1kbq
[17]
PubMed ID11340659
JournalProteins
Year2001
Volume43
Pages420-32
AuthorsCavelier G, Amzel LM
TitleMechanism of NAD(P)H:quinone reductase: Ab initio studies of reduced flavin.
[18]
PubMed ID12147263
JournalArch Biochem Biophys
Year2002
Volume404
Pages254-62
AuthorsAnusevicius Z, Sarlauskas J, Cenas N
TitleTwo-electron reduction of quinones by rat liver NAD(P)H:quinone oxidoreductase: quantitative structure-activity relationships.
[19]
PubMed ID15078100
JournalBiochemistry
Year2004
Volume43
Pages4538-47
AuthorsKwiek JJ, Haystead TA, Rudolph J
TitleKinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines.


createdupdated
2004-10-262009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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