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Identification
HMDB Protein ID HMDBP01689
Secondary Accession Numbers
  • 7026
Name NAD(P)H dehydrogenase [quinone] 1
Synonyms
  1. Azoreductase
  2. DT-diaphorase
  3. DTD
  4. Menadione reductase
  5. NAD(P)H:quinone oxidoreductase 1
  6. Phylloquinone reductase
  7. QR1
  8. Quinone reductase 1
Gene Name NQO1
Protein Type Unknown
Biological Properties
General Function Involved in electron carrier activity
Specific Function The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.
Pathways
  • Doxorubicin Metabolism Pathway
  • Phenytoin (Antiarrhythmic) Action Pathway
  • Ubiquinone and other terpenoid-quinone biosynthesis
  • Vitamin K Metabolism
Reactions
NAD(P)H + a quinone → NAD(P)(+) + a hydroquinone details
Menatetrenone + Hydrogen Ion + NADH → Menaquinol + NAD details
Vitamin K + NADH + Hydrogen Ion → Reduced Vitamin K + NAD details
Vitamin K1 + NADH + Hydrogen Ion → Phylloquinol + NAD details
GO Classification
Biological Process
small molecule metabolic process
regulation of cellular amino acid metabolic process
response to oxidative stress
xenobiotic metabolic process
synaptic transmission, cholinergic
response to toxin
negative regulation of catalytic activity
positive regulation of neuron apoptotic process
nitric oxide biosynthetic process
Cellular Component
cytosol
Function
binding
catalytic activity
electron carrier activity
coenzyme binding
cofactor binding
oxidoreductase activity
Molecular Function
cytochrome-b5 reductase activity
NAD(P)H dehydrogenase (quinone) activity
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 16
Locus 16q22.1
SNPs NQO1
Gene Sequence
>825 bp
ATGGTCGGCAGAAGAGCACTGATCGTACTGGCTCACTCAGAGAGGACCTCCTTCAACTAT
GCCATGAAGGAGGCTGCTGCAGCGGCTTTGAAGAAGAAAGGATGGGAGGTGGTGGAGTCG
GACCTCTATGCCATGAACTTCAATCCCATCATTTCCAGAAAGGACATCACAGGTAAACTG
AAGGACCCTGCGAACTTTCAGTATCCTGCCGAGTCTGTTCTGGCTTATAAAGAAGGCCAT
CTGAGCCCAGATATTGTGGCTGAACAAAAGAAGCTGGAAGCCGCAGACCTTGTGATATTC
CAGTTCCCCCTGCAGTGGTTTGGAGTCCCTGCCATTCTGAAAGGCTGGTTTGAGCGAGTG
TTCATAGGAGAGTTTGCTTACACTTACGCTGCCATGTATGACAAAGGACCCTTCCGGAGT
AAGAAGGCAGTGCTTTCCATCACCACTGGTGGCAGTGGCTCCATGTACTCTCTGCAAGGG
ATCCACGGGGACATGAATGTCATTCTCTGGCCAATTCAGAGTGGCATTCTGCATTTCTGT
GGCTTCCAAGTCTTAGAACCTCAACTGACATATAGCATTGGGCACACTCCAGCAGACGCC
CGAATTCAAATCCTGGAAGGATGGAAGAAACGCCTGGAGAATATTTGGGATGAGACACCA
CTGTATTTTGCTCCAAGCAGCCTCTTTGACCTAAACTTCCAGGCAGGATTCTTAATGAAA
AAAGAGGTACAGGATGAGGAGAAAAACAAGAAATTTGGCCTTTCTGTGGGCCATCACTTG
GGCAAGTCCATCCCAACTGACAACCAGATCAAAGCTAGAAAATGA
Protein Properties
Number of Residues 274
Molecular Weight 30867.405
Theoretical pI 8.886
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>NAD(P)H dehydrogenase [quinone] 1
MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKL
KDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERV
FIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFC
GFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMK
KEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P15559
UniProtKB/Swiss-Prot Entry Name NQO1_HUMAN
PDB IDs
GenBank Gene ID J03934
GeneCard ID NQO1
GenAtlas ID NQO1
HGNC ID HGNC:2874
References
General References
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  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Jaiswal AK, McBride OW, Adesnik M, Nebert DW: Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase. cDNA sequence and localization of gene to chromosome 16. J Biol Chem. 1988 Sep 25;263(27):13572-8. [PubMed:2843525 ]
  5. Jaiswal AK: Human NAD(P)H:quinone oxidoreductase (NQO1) gene structure and induction by dioxin. Biochemistry. 1991 Nov 5;30(44):10647-53. [PubMed:1657151 ]
  6. Skelly JV, Sanderson MR, Suter DA, Baumann U, Read MA, Gregory DS, Bennett M, Hobbs SM, Neidle S: Crystal structure of human DT-diaphorase: a model for interaction with the cytotoxic prodrug 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954). J Med Chem. 1999 Oct 21;42(21):4325-30. [PubMed:10543876 ]
  7. Faig M, Bianchet MA, Talalay P, Chen S, Winski S, Ross D, Amzel LM: Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: species comparison and structural changes with substrate binding and release. Proc Natl Acad Sci U S A. 2000 Mar 28;97(7):3177-82. [PubMed:10706635 ]
  8. Winski SL, Faig M, Bianchet MA, Siegel D, Swann E, Fung K, Duncan MW, Moody CJ, Amzel LM, Ross D: Characterization of a mechanism-based inhibitor of NAD(P)H:quinone oxidoreductase 1 by biochemical, X-ray crystallographic, and mass spectrometric approaches. Biochemistry. 2001 Dec 18;40(50):15135-42. [PubMed:11735396 ]
  9. Faig M, Bianchet MA, Winski S, Hargreaves R, Moody CJ, Hudnott AR, Ross D, Amzel LM: Structure-based development of anticancer drugs: complexes of NAD(P)H:quinone oxidoreductase 1 with chemotherapeutic quinones. Structure. 2001 Aug;9(8):659-67. [PubMed:11587640 ]
  10. Asher G, Dym O, Tsvetkov P, Adler J, Shaul Y: The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol. Biochemistry. 2006 May 23;45(20):6372-8. [PubMed:16700548 ]
  11. Traver RD, Horikoshi T, Danenberg KD, Stadlbauer TH, Danenberg PV, Ross D, Gibson NW: NAD(P)H:quinone oxidoreductase gene expression in human colon carcinoma cells: characterization of a mutation which modulates DT-diaphorase activity and mitomycin sensitivity. Cancer Res. 1992 Feb 15;52(4):797-802. [PubMed:1737339 ]
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