NAD(P)H dehydrogenase, quinone 2

NAD(P)H dehydrogenase, quinone 2, also known as QR2, is a protein that in humans is encoded by the NQO2 gene. It is a phase II detoxification enzyme which can carry out two or four electron reductions. Its mechanism of reduction is via a covalently bound zinc ion and a cocrystalized FAD. NQO2 contains two chains homologous in AA sequence but 7% different in structure. As a result, NQO2 contains two similar yet unique active sites. An important function of NQO2 is its activation on NRH. NQO2 can be inhibited by resveratrol.[5]

NQO2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1QR2, 1SG0, 1XI2, 1ZX1, 2BZS, 2QMY, 2QMZ, 2QR2, 2QWX, 2QX4, 2QX6, 2QX8, 2QX9, 3FW1, 3G5M, 3GAM, 3NFR, 3NHF, 3NHJ, 3NHK, 3NHL, 3NHP, 3NHR, 3NHS, 3NHU, 3NHW, 3NHY, 3O2N, 3O73, 3OVM, 3OWH, 3OWX, 3OX1, 3OX2, 3OX3, 3TE7, 3TEM, 3TZB, 3UXE, 3UXH, 4FGJ, 4FGK, 4FGL, 4GQI, 4GR9, 4QOD, 4QOE, 4QOF, 4QOG, 4QOH, 4QOI, 4QOJ, 4U7F, 4U7G, 4U7H, 4XDG, 4XDH, 4ZVL, 4ZVM, 4ZVK, 5LBT, 5LBU, 5BUC, 4ZVN
Identifiers
Aliases	NQO2, Nqo2, NMO2, Nmor2, Ox2, DHQV, DIA6, QR2, NAD(P)H quinone dehydrogenase 2, N-ribosyldihydronicotinamide:quinone reductase 2
External IDs	OMIM: 160998 MGI: 104513 HomoloGene: 696 GeneCards: NQO2
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p25.2 Start 2,987,987 bp[1] End 3,028,869 bp[1]
Gene location (Mouse) Chr. Chromosome 13 (mouse)[2] Band 13 A3.3|13 14.01 cM Start 33,964,687 bp[2] End 33,988,443 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • metal ion binding • dihydronicotinamide riboside quinone reductase activity • zinc ion binding • electron transfer activity • oxidoreductase activity • oxidoreductase activity, acting on other nitrogenous compounds as donors • chloride ion binding • protein homodimerization activity • FAD binding • melatonin binding • resveratrol binding • NAD(P)H dehydrogenase (quinone) activity Cellular component • extracellular exosome • nucleoplasm • cytoplasm • cytosol Biological process • memory • positive regulation of neuron apoptotic process • positive regulation of vascular smooth muscle cell proliferation • positive regulation of ERK1 and ERK2 cascade • positive regulation of reactive oxygen species metabolic process • xenobiotic metabolic process • oxidation-reduction process • electron transport chain Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4835	18105
Ensembl	ENSG00000124588	ENSMUSG00000046949
UniProt	P16083	Q9JI75
RefSeq (mRNA)	NM_000904 NM_001290221 NM_001290222 NM_001318940	NM_001163239 NM_001163241 NM_001163242 NM_020282
RefSeq (protein)	NP_000895 NP_001277150 NP_001277151 NP_001305869	NP_001156711 NP_001156713 NP_001156714 NP_064678
Location (UCSC)	Chr 6: 2.99 – 3.03 Mb	Chr 13: 33.96 – 33.99 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

References

1. GRCh38: Ensembl release 89: ENSG00000124588 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000046949 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: NQO2 NAD(P)H dehydrogenase, quinone 2".

Further reading

• Jaiswal AK, Burnett P, Adesnik M, McBride OW (1990). "Nucleotide and deduced amino acid sequence of a human cDNA (NQO2) corresponding to a second member of the NAD(P)H:quinone oxidoreductase gene family. Extensive polymorphism at the NQO2 gene locus on chromosome 6". Biochemistry. 29 (7): 1899–906. doi:10.1021/bi00459a034. PMID 1691923.
• Jaiswal AK (1994). "Human NAD(P)H:quinone oxidoreductase2. Gene structure, activity, and tissue-specific expression". J. Biol. Chem. 269 (20): 14502–8. PMID 8182056.
• Zhao Q, Yang XL, Holtzclaw WD, Talalay P (1997). "Unexpected genetic and structural relationships of a long-forgotten flavoenzyme to NAD(P)H:quinone reductase (DT-diaphorase)". Proc. Natl. Acad. Sci. U.S.A. 94 (5): 1669–74. doi:10.1073/pnas.94.5.1669. PMC 19974. PMID 9050836.
• Wu K, Knox R, Sun XZ, et al. (1997). "Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase". Arch. Biochem. Biophys. 347 (2): 221–8. doi:10.1006/abbi.1997.0344. PMID 9367528.
• Foster CE, Bianchet MA, Talalay P, et al. (1999). "Crystal structure of human quinone reductase type 2, a metalloflavoprotein". Biochemistry. 38 (31): 9881–6. doi:10.1021/bi990799v. PMID 10433694.
• Jaiswal AK, Bell DW, Radjendirane V, Testa JR (1999). "Localization of human NQO1 gene to chromosome 16q22 and NQO2-6p25 and associated polymorphisms". Pharmacogenetics. 9 (3): 413–8. doi:10.1097/00008571-199906000-00020. PMID 10471077.
• 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.
• Strassburg A, Strassburg CP, Manns MP, Tukey RH (2002). "Differential gene expression of NAD(P)H:quinone oxidoreductase and NRH:quinone oxidoreductase in human hepatocellular and biliary tissue". Mol. Pharmacol. 61 (2): 320–5. doi:10.1124/mol.61.2.320. PMID 11809856.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Okubo T, Harada S, Higuchi S, Matsushita S (2004). "Association analyses between polymorphisms of the phase II detoxification enzymes (GSTM1, NQO1, NQO2) and alcohol withdrawal symptoms". Alcohol. Clin. Exp. Res. 27 (8 Suppl): 68S–71S. doi:10.1097/01.ALC.0000078616.63296.41. PMID 12960511.
• Ostrousky O, Meged S, Loewenthal R, et al. (2004). "NQO2 gene is associated with clozapine-induced agranulocytosis". Tissue Antigens. 62 (6): 483–91. doi:10.1046/j.1399-0039.2003.00133.x. PMID 14617031.
• Harada S, Tachikawa H, Kawanishi Y (2005). "A possible association between an insertion/deletion polymorphism of the NQO2 gene and schizophrenia". Psychiatr. Genet. 13 (4): 205–9. doi:10.1097/01.ypg.0000071601.59979.47 (inactive 2020-05-11). PMID 14639047.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Kwiek JJ, Haystead TA, Rudolph J (2004). "Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines". Biochemistry. 43 (15): 4538–47. doi:10.1021/bi035923w. PMID 15078100.
• Buryanovskyy L, Fu Y, Boyd M, et al. (2004). "Crystal structure of quinone reductase 2 in complex with resveratrol". Biochemistry. 43 (36): 11417–26. doi:10.1021/bi049162o. PMC 3650734. PMID 15350128.
• Wang W, Jaiswal AK (2005). "Sp3 repression of polymorphic human NRH:quinone oxidoreductase 2 gene promoter". Free Radic. Biol. Med. 37 (8): 1231–43. doi:10.1016/j.freeradbiomed.2004.06.042. PMID 15451063.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Hsieh TC, Wang Z, Hamby CV, Wu JM (2005). "Inhibition of melanoma cell proliferation by resveratrol is correlated with upregulation of quinone reductase 2 and p53". Biochem. Biophys. Res. Commun. 334 (1): 223–30. doi:10.1016/j.bbrc.2005.06.073. PMID 15993843.
• Fu Y, Buryanovskyy L, Zhang Z (2005). "Crystal structure of quinone reductase 2 in complex with cancer prodrug CB1954". Biochem. Biophys. Res. Commun. 336 (1): 332–8. doi:10.1016/j.bbrc.2005.08.081. PMID 16129418.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.

External links

• Overview of all the structural information available in the PDB for UniProt: P16083 (Ribosyldihydronicotinamide dehydrogenase [quinone]) at the PDBe-KB.