EzCatDB: S00343
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DB codeS00343
CATH domainDomain 13.40.50.360 : Rossmann foldCatalytic domain
E.C.1.6.5.2
CSA1d4a
MACiEM0003

CATH domainRelated DB codes (homologues)
3.40.50.360 : Rossmann foldS00522,M00006,M00154

Enzyme Name
UniProtKBKEGG

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
RefSeqNP_000894.1 (Protein)
NM_000903.2 (DNA/RNA sequence)
NP_001020604.1 (Protein)
NM_001025433.1 (DNA/RNA sequence)
NP_001020605.1 (Protein)
NM_001025434.1 (DNA/RNA sequence)
NP_032732.3 (Protein)
NM_008706.5 (DNA/RNA sequence)
NP_058696.2 (Protein)
NM_017000.3 (DNA/RNA sequence)
PfamPF02525 (Flavodoxin_2)
[Graphical view]
PF02525 (Flavodoxin_2)
[Graphical view]
PF02525 (Flavodoxin_2)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00100Biosynthesis of steroids

UniProtKB: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.

Compound table: links to PDB-related databases & PoSSuM

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)
ChEBI16238
29105
16474
16908
15378
16509
18009
15846
17594
PubChem643975
32051
5884
439153
1038
4650
5886
5893
785
                 
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 UniProtKBP15559
[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
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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 2008)
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)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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