S00343
type: Enzyme
cath: Rossmann fold
ec: https://purl.uniprot.org/enzyme/1.6.5.2
csa: 1d4a
macie: M0003
uniprot: P15559
uniprot: Q64669
uniprot: P05982
kegg enzyme: NAD(P)H dehydrogenase (quinone)
kegg enzyme: menadione reductase
kegg enzyme: phylloquinone reductase
kegg pathway: Biosynthesis of steroids
kegg cofactor: FAD
kegg cofactor: Zinc
kegg substrate: NADPH
kegg substrate: NADH
kegg substrate: H+
kegg substrate: Quinone
kegg product: NADP+
kegg product: NAD+
kegg product: Hydroquinone
pdb: 1d4aA
pdb: 1d4aB
pdb: 1d4aC
pdb: 1d4aD
pdb: 1dxoA
pdb: 1dxoB
pdb: 1dxoC
pdb: 1dxoD
pdb: 1dxqA
pdb: 1dxqB
pdb: 1dxqC
pdb: 1dxqD
pdb: 1gg5A
pdb: 1gg5B
pdb: 1gg5C
pdb: 1gg5D
pdb: 1h66A
pdb: 1h66B
pdb: 1h66C
pdb: 1h66D
pdb: 1h69A
pdb: 1h69B
pdb: 1h69C
pdb: 1h69D
pdb: 1kboA
pdb: 1kboB
pdb: 1kboC
pdb: 1kboD
pdb: 1kbqA
pdb: 1kbqB
pdb: 1kbqC
pdb: 1kbqD
pdb: 1qbgA
pdb: 1qbgB
pdb: 1qbgC
pdb: 1qbgD
pdb: 1qrdA
pdb: 1qrdB
active site residues resources: Molecular basis of the catalytic differences among DT-diaphorase of human, rat, and mouse.
active site residues resources: 1h66
references: Bioreductive activation of mitomycin C by DT-diaphorase.
references: Antioxidant and prooxidant functions of DT-diaphorase in quinone metabolism.
references: The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction.
references: Molecular basis of the catalytic differences among DT-diaphorase of human, rat, and mouse.
references: Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase).
references: Structure and mechanism of cytosolic quinone reductases.
references: Crystal structure of human quinone reductase type 2, a metalloflavoprotein.
references: Crystal structure of human DT-diaphorase: a model for interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954).
references: Molecular characterization of binding of substrates and inhibitors to DT-diaphorase: combined approach involving site-directed mutagenesis, inhibitor-binding analysis, and computer modeling.
references: Structure-function studies of DT-diaphorase (NQO1) and NRH: quinone oxidoreductase (NQO2).
references: Mechanisms of action of quinone-containing alkylating agents. I: NQO1-directed drug development.
references: Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release.
references: Flavoenzymes: diverse catalysts with recurrent features.
references: Structures of mammalian cytosolic quinone reductases.
references: Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones.
references: Characterization of a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1 by biochemical, X-ray crystallographic, and mass spectrometric approaches.
references: Mechanism of NAD(P)H:quinone reductase: Ab initio studies of reduced flavin.
references: Two-electron reduction of quinones by rat liver NAD(P)H:quinone oxidoreductase: quantitative structure-activity relationships.
references: Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines.

Rossmann fold
type: Cath
references: http://www.cathdb.info/version/latest/superfamily/3.40.50.360
catalytic domain: index.html

Biosynthesis of steroids
type: KeggPathway
references: KEGG:MAP00100

FAD
type: KeggCofactor
references: KEGG:C00016
compound type: amide group
compound type: amine group
compound type: aromatic ring (only carbon atom)
compound type: aromatic ring (with nitrogen atoms)
compound type: carbohydrate
compound type: nucleotide
references: CHEBI:16238
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Zinc
type: KeggCofactor
references: KEGG:C00038
compound type: heavy metal
references: CHEBI:29105
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADPH
type: KeggSubstrate
references: KEGG:C00005
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16474
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADH
type: KeggSubstrate
references: KEGG:C00004
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:16908
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

H+
type: KeggSubstrate
references: KEGG:C00080
compound type: others
references: CHEBI:15378
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Quinone
type: KeggSubstrate
references: KEGG:C00472
compound type: aromatic ring (only carbon atom)
references: CHEBI:16509
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NADP+
type: KeggProduct
references: KEGG:C00006
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:18009
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

NAD+
type: KeggProduct
references: KEGG:C00003
compound type: amide group
compound type: amine group
compound type: nucleotide
references: CHEBI:15846
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

Hydroquinone
type: KeggProduct
references: KEGG:C00530
compound type: aromatic ring (only carbon atom)
references: CHEBI:17594
references: http://pubchem.ncbi.nlm.nih.gov/summary/summary.cgi

1d4aA
type: Pdb
references: 1d4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d4a
catalytic residue: GLY 149;TYR 155;HIS 161

1d4aB
type: Pdb
references: 1d4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d4a
catalytic residue: GLY 149;TYR 155;HIS 161

1d4aC
type: Pdb
references: 1d4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d4a
catalytic residue: GLY 149;TYR 155;HIS 161

1d4aD
type: Pdb
references: 1d4a
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1d4a
catalytic residue: GLY 149;TYR 155;HIS 161

1dxoA
type: Pdb
references: 1dxo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxo
catalytic residue: GLY 149;TYR 155;HIS 161

1dxoB
type: Pdb
references: 1dxo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxo
catalytic residue: GLY 149;TYR 155;HIS 161

1dxoC
type: Pdb
references: 1dxo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxo
catalytic residue: GLY 149;TYR 155;HIS 161

1dxoD
type: Pdb
references: 1dxo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxo
catalytic residue: GLY 149;TYR 155;HIS 161

1dxqA
type: Pdb
references: 1dxq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxq
catalytic residue: GLY 149;TYR 155;HIS 161

1dxqB
type: Pdb
references: 1dxq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxq
catalytic residue: GLY 149;TYR 155;HIS 161

1dxqC
type: Pdb
references: 1dxq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxq
catalytic residue: GLY 149;TYR 155;HIS 161

1dxqD
type: Pdb
references: 1dxq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1dxq
catalytic residue: GLY 149;TYR 155;HIS 161

1gg5A
type: Pdb
references: 1gg5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gg5
catalytic residue: GLY 149;TYR 155;HIS 161

1gg5B
type: Pdb
references: 1gg5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gg5
catalytic residue: GLY 149;TYR 155;HIS 161

1gg5C
type: Pdb
references: 1gg5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gg5
catalytic residue: GLY 149;TYR 155;HIS 161

1gg5D
type: Pdb
references: 1gg5
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1gg5
catalytic residue: GLY 149;TYR 155;HIS 161

1h66A
type: Pdb
references: 1h66
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h66
catalytic residue: GLY 149;TYR 155;HIS 161

1h66B
type: Pdb
references: 1h66
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h66
catalytic residue: GLY 149;TYR 155;HIS 161

1h66C
type: Pdb
references: 1h66
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h66
catalytic residue: GLY 149;TYR 155;HIS 161

1h66D
type: Pdb
references: 1h66
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h66
catalytic residue: GLY 149;TYR 155;HIS 161

1h69A
type: Pdb
references: 1h69
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h69
catalytic residue: GLY 149;TYR 155;HIS 161

1h69B
type: Pdb
references: 1h69
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h69
catalytic residue: GLY 149;TYR 155;HIS 161

1h69C
type: Pdb
references: 1h69
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h69
catalytic residue: GLY 149;TYR 155;HIS 161

1h69D
type: Pdb
references: 1h69
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1h69
catalytic residue: GLY 149;TYR 155;HIS 161

1kboA
type: Pdb
references: 1kbo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kbo
catalytic residue: GLY 149;TYR 155;HIS 161

1kboB
type: Pdb
references: 1kbo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kbo
catalytic residue: GLY 149;TYR 155;HIS 161

1kboC
type: Pdb
references: 1kbo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kbo
catalytic residue: GLY 149;TYR 155;HIS 161

1kboD
type: Pdb
references: 1kbo
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kbo
catalytic residue: GLY 149;TYR 155;HIS 161

1kbqA
type: Pdb
references: 1kbq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kbq
catalytic residue: GLY 149;TYR 155;HIS 161

1kbqB
type: Pdb
references: 1kbq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kbq
catalytic residue: GLY 149;TYR 155;HIS 161

1kbqC
type: Pdb
references: 1kbq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kbq
catalytic residue: GLY 149;TYR 155;HIS 161

1kbqD
type: Pdb
references: 1kbq
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1kbq
catalytic residue: GLY 149;TYR 155;HIS 161

1qbgA
type: Pdb
references: 1qbg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbg
catalytic residue: GLY 149;TYR 155;HIS 161

1qbgB
type: Pdb
references: 1qbg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbg
catalytic residue: GLY 149;TYR 155;HIS 161

1qbgC
type: Pdb
references: 1qbg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbg
catalytic residue: GLY 149;TYR 155;HIS 161

1qbgD
type: Pdb
references: 1qbg
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qbg
catalytic residue: GLY 149;TYR 155;HIS 161

1qrdA
type: Pdb
references: 1qrd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qrd
catalytic residue: GLY 149;TYR 155;HIS 161

1qrdB
type: Pdb
references: 1qrd
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: PDB:1qrd
catalytic residue: GLY 149;TYR 155;HIS 161

Bioreductive activation of mitomycin C by DT-diaphorase.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/1510975
journal: Biochemistry
volume: 31
pages: 7879-85
published year: 1992
authors:
  item: Siegel D
  item: Beall H
  item: Senekowitsch C
  item: Kasai M
  item: Arai H
  item: Gibson NW
  item: Ross D

Antioxidant and prooxidant functions of DT-diaphorase in quinone metabolism.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/7530954
journal: Biochem Pharmacol
volume: 49
pages: 127-40
published year: 1995
authors:
  item: Cadenas E

The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: mechanism of the two-electron reduction.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/7568029
journal: Proc Natl Acad Sci U S A
volume: 92
pages: 8846-50
published year: 1995
authors:
  item: Li R
  item: Bianchet MA
  item: Talalay P
  item: Amzel LM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Molecular basis of the catalytic differences among DT-diaphorase of human, rat, and mouse.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/8999809
journal: J Biol Chem
volume: 272
pages: 1437-9
published year: 1997
authors:
  item: Chen S
  item: Knox R
  item: Wu K
  item: Deng PS
  item: Zhou D
  item: Bianchet MA
  item: Amzel LM

Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/9050836
journal: Proc Natl Acad Sci U S A
volume: 94
pages: 1669-74
published year: 1997
authors:
  item: Zhao Q
  item: Yang XL
  item: Holtzclaw WD
  item: Talalay P

Structure and mechanism of cytosolic quinone reductases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10917652
journal: Biochem Soc Trans
volume: 27
pages: 610-5
published year: 1999
authors:
  item: Bianchet MA
  item: Foster C
  item: Faig M
  item: Talalay P
  item: Amzel LM

Crystal structure of human quinone reductase type 2, a metalloflavoprotein.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10433694
journal: Biochemistry
volume: 38
pages: 9881-6
published year: 1999
authors:
  item: Foster CE
  item: Bianchet MA
  item: Talalay P
  item: Zhao Q
  item: Amzel LM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Crystal structure of human DT-diaphorase: a model for interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954).
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/10543876
journal: J Med Chem
volume: 42
pages: 4325-30
published year: 1999
authors:
  item: Skelly JV
  item: Sanderson MR
  item: Suter DA
  item: Baumann U
  item: Read MA
  item: Gregory DS
  item: Bennett M
  item: Hobbs SM
  item: Neidle S
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Molecular characterization of binding of substrates and inhibitors to DT-diaphorase: combined approach involving site-directed mutagenesis, inhibitor-binding analysis, and computer modeling.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10419545
journal: Mol Pharmacol
volume: 56
pages: 272-8
published year: 1999
authors:
  item: Chen S
  item: Wu K
  item: Zhang D
  item: Sherman M
  item: Knox R
  item: Yang CS

Structure-function studies of DT-diaphorase (NQO1) and NRH: quinone oxidoreductase (NQO2).
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11035256
journal: Free Radic Biol Med
volume: 29
pages: 276-84
published year: 2000
authors:
  item: Chen S
  item: Wu K
  item: Knox R

Mechanisms of action of quinone-containing alkylating agents. I: NQO1-directed drug development.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10877993
journal: Front Biosci
volume: 5
pages: D639-48
published year: 2000
authors:
  item: Beall HD
  item: Winski SI

Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release.
type: BibliographicResource
comment: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
medline id: 20202608
references: http://www.ncbi.nlm.nih.gov/pubmed/10706635
journal: Proc Natl Acad Sci U S A
volume: 97
pages: 3177-82
published year: 2000
authors:
  item: Faig M
  item: Bianchet MA
  item: Talalay P
  item: Chen S
  item: Winski S
  item: Ross D
  item: Amzel LM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl
references: P15559

Flavoenzymes: diverse catalysts with recurrent features.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/10694883
journal: Trends Biochem Sci
volume: 25
pages: 126-32
published year: 2000
authors:
  item: Fraaije MW
  item: Mattevi A

Structures of mammalian cytosolic quinone reductases.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11035252
journal: Free Radic Biol Med
volume: 29
pages: 241-5
published year: 2000
authors:
  item: Foster CE
  item: Bianchet MA
  item: Talalay P
  item: Faig M
  item: Amzel LM

Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11587640
journal: Structure (Camb)
volume: 9
pages: 659-67
published year: 2001
authors:
  item: Faig M
  item: Bianchet MA
  item: Winski S
  item: Hargreaves R
  item: Moody CJ
  item: Hudnott AR
  item: Ross D
  item: Amzel LM
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Characterization of a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1 by biochemical, X-ray crystallographic, and mass spectrometric approaches.
type: BibliographicResource
comment: X-ray crystallography
references: http://www.ncbi.nlm.nih.gov/pubmed/11735396
journal: Biochemistry
volume: 40
pages: 15135-42
published year: 2001
authors:
  item: Winski SL
  item: Faig M
  item: Bianchet MA
  item: Siegel D
  item: Swann E
  item: Fung K
  item: Duncan MW
  item: Moody CJ
  item: Amzel LM
  item: Ross D
references: http://www.ebi.ac.uk/thornton-srv/databases/cgi-bin/pdbsum/GetPage.pl

Mechanism of NAD(P)H:quinone reductase: Ab initio studies of reduced flavin.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/11340659
journal: Proteins
volume: 43
pages: 420-32
published year: 2001
authors:
  item: Cavelier G
  item: Amzel LM

Two-electron reduction of quinones by rat liver NAD(P)H:quinone oxidoreductase: quantitative structure-activity relationships.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/12147263
journal: Arch Biochem Biophys
volume: 404
pages: 254-62
published year: 2002
authors:
  item: Anusevicius Z
  item: Sarlauskas J
  item: Cenas N

Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines.
type: BibliographicResource
references: http://www.ncbi.nlm.nih.gov/pubmed/15078100
journal: Biochemistry
volume: 43
pages: 4538-47
published year: 2004
authors:
  item: Kwiek JJ
  item: Haystead TA
  item: Rudolph J

quinone reductase
type: KeggEnzyme

dehydrogenase, reduced nicotinamide adenine dinucleotide (phosphate,quinone)
type: KeggEnzyme

DT-diaphorase
type: KeggEnzyme

flavoprotein NAD(P)H-quinone reductase
type: KeggEnzyme

menadione oxidoreductase
type: KeggEnzyme

NAD(P)H dehydrogenase
type: KeggEnzyme

NAD(P)H menadione reductase
type: KeggEnzyme

NAD(P)H-quinone dehydrogenase
type: KeggEnzyme

NAD(P)H-quinone oxidoreductase
type: KeggEnzyme

NAD(P)H: (quinone-acceptor)oxidoreductase
type: KeggEnzyme

NAD(P)H: menadione oxidoreductase
type: KeggEnzyme

NADH-menadione reductase
type: KeggEnzyme

naphthoquinone reductase
type: KeggEnzyme

p-benzoquinone reductase
type: KeggEnzyme

reduced NAD(P)H dehydrogenase
type: KeggEnzyme

viologen accepting pyridine nucleotide oxidoreductase
type: KeggEnzyme

vitamin K reductase
type: KeggEnzyme

diaphorase
type: KeggEnzyme

reduced nicotinamide-adenine dinucleotide (phosphate) dehydrogenase
type: KeggEnzyme

vitamin-K reductase
type: KeggEnzyme

NAD(P)H2 dehydrogenase (quinone)
type: KeggEnzyme

NQO1
type: KeggEnzyme

QR1
type: KeggEnzyme

NAD(P)H:(quinone-acceptor) oxidoreductase
type: KeggEnzyme

Analogue
compound: Quinone
pdb: 1dxoA
ligand het code: DQN

Analogue
compound: Quinone
pdb: 1dxoB
ligand het code: DQN

Analogue
compound: Quinone
pdb: 1dxoC
ligand het code: 2xDQN

Analogue
compound: Quinone
pdb: 1gg5A
ligand het code: E09

Analogue
compound: Quinone
pdb: 1gg5B
ligand het code: E09

Analogue
compound: Quinone
pdb: 1gg5C
ligand het code: E09

Analogue
compound: Quinone
pdb: 1gg5D
ligand het code: E09

Analogue
compound: Quinone
pdb: 1h66A
ligand het code: RH1

Analogue
compound: Quinone
pdb: 1h66B
ligand het code: RH1

Analogue
compound: Quinone
pdb: 1h66C
ligand het code: RH1

Analogue
compound: Quinone
pdb: 1h66D
ligand het code: RH1

Analogue
compound: Quinone
pdb: 1h69A
ligand het code: ARH

Analogue
compound: Quinone
pdb: 1h69B
ligand het code: ARH

Analogue
compound: Quinone
pdb: 1h69C
ligand het code: ARH

Analogue
compound: Quinone
pdb: 1h69D
ligand het code: ARH

Analogue
compound: Quinone
pdb: 1kboA
ligand het code: 340

Analogue
compound: Quinone
pdb: 1kboB
ligand het code: 340

Analogue
compound: Quinone
pdb: 1kboC
ligand het code: 340

Analogue
compound: Quinone
pdb: 1kboD
ligand het code: 340

Analogue
compound: Quinone
pdb: 1kbqA
ligand het code: 936

Analogue
compound: Quinone
pdb: 1kbqB
ligand het code: 936

Analogue
compound: Quinone
pdb: 1kbqC
ligand het code: 936

Analogue
compound: Quinone
pdb: 1kbqD
ligand het code: 936

Analogue
compound: Quinone
pdb: 1qrdA
ligand het code: DQN

Analogue
compound: Quinone
pdb: 1qrdB
ligand het code: DQN

ReferenceForCatalyticMechanism
reference index: 3
reference section: Fig.8, p.8849-8850

ReferenceForCatalyticMechanism
reference index: 6
reference section: p.612-614

ReferenceForCatalyticMechanism
reference index: 7
reference section: p.9985-9986

ReferenceForCatalyticMechanism
reference index: 10
reference section: p.278-279

ReferenceForCatalyticMechanism
reference index: 13
reference section: Fig.1, Fig.4, p.130-131

ReferenceForCatalyticMechanism
reference index: 14
reference section: p.244

ReferenceForCatalyticMechanism
reference index: 15
reference section: p.664-665

ReferenceForCatalyticMechanism
reference index: 19
reference section: Fig.8