NAD(P)H dehydrogenase (quinone 1)

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NAD(P)H dehydrogenase, quinone 1
File:PBB Protein NQO1 image.jpg
PDB rendering based on 1d4a.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols NQO1 ; DHQU; DIA4; DTD; NMOR1; NMORI; QR1
External IDs Template:OMIM5 Template:MGI HomoloGene: 695
RNA expression pattern
File:PBB GE NQO1 201468 s at tn.png
File:PBB GE NQO1 201467 s at tn.png
File:PBB GE NQO1 210519 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

NAD(P)H dehydrogenase, quinone 1, also known as NQO1, is a human gene.

This gene is a member of the NAD(P)H dehydrogenase (quinone) family and encodes a cytoplasmic 2-electron reductase. This FAD-binding protein forms homodimers and reduces quinones to hydroquinones. This protein's enzymatic activity prevents the one electron reduction of quinones that results in the production of radical species. Mutations in this gene have been associated with tardive dyskinesia (TD), an increased risk of hematotoxicity after exposure to benzene, and susceptibility to various forms of cancer. Altered expression of this protein has been seen in many tumors and is also associated with Alzheimer's disease (AD). Alternate transcriptional splice variants, encoding different isoforms, have been characterized.[1]

References

  1. ↑ "Entrez Gene: NQO1 NAD(P)H dehydrogenase, quinone 1".

Further reading

  • Vasiliou V, Ross D, Nebert DW (2006). "Update of the NAD(P)H:quinone oxidoreductase (NQO) gene family". Hum. Genomics. 2 (5): 329–35. PMID 16595077.
  • Li Y, Jaiswal AK (1992). "Regulation of human NAD(P)H:quinone oxidoreductase gene. Role of AP1 binding site contained within human antioxidant response element". J. Biol. Chem. 267 (21): 15097–104. PMID 1340765.
  • Jaiswal AK (1991). "Human NAD(P)H:quinone oxidoreductase (NQO1) gene structure and induction by dioxin". Biochemistry. 30 (44): 10647–53. PMID 1657151.
  • Traver RD, Horikoshi T, Danenberg KD; et al. (1992). "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. 52 (4): 797–802. PMID 1737339.
  • Chen LZ, Harris PC, Apostolou S; et al. (1991). "A refined physical map of the long arm of human chromosome 16". Genomics. 10 (2): 308–12. PMID 2071140.
  • Jaiswal AK, McBride OW, Adesnik M, Nebert DW (1988). "Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase. cDNA sequence and localization of gene to chromosome 16". J. Biol. Chem. 263 (27): 13572–8. PMID 2843525.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
  • Rothman N, Smith MT, Hayes RB; et al. (1997). "Benzene poisoning, a risk factor for hematological malignancy, is associated with the NQO1 609C-->T mutation and rapid fractional excretion of chlorzoxazone". Cancer Res. 57 (14): 2839–42. PMID 9230185.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.
  • Smiley JF, Levey AI, Mesulam MM (1998). "Infracortical interstitial cells concurrently expressing m2-muscarinic receptors, acetylcholinesterase and nicotinamide adenine dinucleotide phosphate-diaphorase in the human and monkey cerebral cortex". Neuroscience. 84 (3): 755–69. PMID 9579781.
  • Moran JL, Siegel D, Ross D (1999). "A potential mechanism underlying the increased susceptibility of individuals with a polymorphism in NAD(P)H:quinone oxidoreductase 1 (NQO1) to benzene toxicity". Proc. Natl. Acad. Sci. U.S.A. 96 (14): 8150–5. PMID 10393963.
  • Kristiansen OP, Larsen ZM, Johannesen J; et al. (1999). "No linkage of P187S polymorphism in NAD(P)H: quinone oxidoreductase (NQO1/DIA4) and type 1 diabetes in the Danish population. DIEGG and DSGD. Danish IDDM Epidemiology and Genetics Group and The Danish Study Group of Diabetes in Childhood". Hum. Mutat. 14 (1): 67–70. doi:10.1002/(SICI)1098-1004(1999)14:1<67::AID-HUMU8>3.0.CO;2-5. PMID 10447260.
  • Eliasson M, Boström M, DePierre JW (1999). "Levels and subcellular distributions of detoxifying enzymes in the ovarian corpus luteum of the pregnant and non-pregnant pig". Biochem. Pharmacol. 58 (8): 1287–92. PMID 10487530.
  • Skelly JV, Sanderson MR, Suter DA; et al. (1999). "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. 42 (21): 4325–30. PMID 10543876.
  • Faig M, Bianchet MA, Talalay P; et al. (2000). "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. 97 (7): 3177–82. doi:10.1073/pnas.050585797. PMID 10706635.
  • Harada S, Fujii C, Hayashi A, Ohkoshi N (2001). "An association between idiopathic Parkinson's disease and polymorphisms of phase II detoxification enzymes: glutathione S-transferase M1 and quinone oxidoreductase 1 and 2". Biochem. Biophys. Res. Commun. 288 (4): 887–92. doi:10.1006/bbrc.2001.5868. PMID 11688992.
  • Siegel D, Ryder J, Ross D (2001). "NAD(P)H: quinone oxidoreductase 1 expression in human bone marrow endothelial cells". Toxicol. Lett. 125 (1–3): 93–8. PMID 11701227.
  • Anwar A, Siegel D, Kepa JK, Ross D (2002). "Interaction of the molecular chaperone Hsp70 with human NAD(P)H:quinone oxidoreductase 1". J. Biol. Chem. 277 (16): 14060–7. doi:10.1074/jbc.M111576200. PMID 11821413.
  • Winski SL, Koutalos Y, Bentley DL, Ross D (2002). "Subcellular localization of NAD(P)H:quinone oxidoreductase 1 in human cancer cells". Cancer Res. 62 (5): 1420–4. PMID 11888914.
  • Begleiter A, Lange L (2002). "Lack of NQO1 induction in human tumor cells is not due to changes in the promoter region of the gene". Int. J. Oncol. 20 (4): 835–8. PMID 11894133.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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