
Health Dictionary
Reliable, easy-to-read patient information on common medical conditions ā written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
NAD(P)H dehydrogenase, quinone 2
Introduction
NAD(P)H dehydrogenase, quinone 2, also known as NQO2 or QR2, is a human 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.[1]
Further reading
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): 1899ā906. doi:10.1021/bi00459a034. PMIDĀ 1691923.
- Jaiswal AK (1994). “Human NAD(P)H:quinone oxidoreductase2. Gene structure, activity, and tissue-specific expression”. J. Biol. Chem. 269 (20): 14502ā8. PMIDĀ 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): 1669ā74. doi:10.1073/pnas.94.5.1669. PMCĀ 19974. PMIDĀ 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): 221ā8. doi:10.1006/abbi.1997.0344. PMIDĀ 9367528.
- Foster CE, Bianchet MA, Talalay P, et al. (1999). “Crystal structure of human quinone reductase type 2, a metalloflavoprotein”. Biochemistry. 38 (31): 9881ā6. doi:10.1021/bi990799v. PMIDĀ 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): 413ā8. doi:10.1097/00008571-199906000-00020. PMIDĀ 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): 887ā92. doi:10.1006/bbrc.2001.5868. PMIDĀ 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): 320ā5. doi:10.1124/mol.61.2.320. PMIDĀ 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): 16899ā903. doi:10.1073/pnas.242603899. PMCĀ 139241. PMIDĀ 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): 68Sā71S. doi:10.1097/01.ALC.0000078616.63296.41. PMIDĀ 12960511.
- Ostrousky O, Meged S, Loewenthal R, et al. (2004). “NQO2 gene is associated with clozapine-induced agranulocytosis”. Tissue Antigens. 62 (6): 483ā91. doi:10.1046/j.1399-0039.2003.00133.x. PMIDĀ 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): 205ā9. doi:10.1097/01.ypg.0000071601.59979.47. PMIDĀ 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): 40ā5. doi:10.1038/ng1285. PMIDĀ 14702039.
- Kwiek JJ, Haystead TA, Rudolph J (2004). “Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines”. Biochemistry. 43 (15): 4538ā47. doi:10.1021/bi035923w. PMIDĀ 15078100.
- Buryanovskyy L, Fu Y, Boyd M, et al. (2004). “Crystal structure of quinone reductase 2 in complex with resveratrol”. Biochemistry. 43 (36): 11417ā26. doi:10.1021/bi049162o. PMCĀ 3650734. PMIDĀ 15350128.
- Wang W, Jaiswal AK (2005). “Sp3 repression of polymorphic human NRH:quinone oxidoreductase 2 gene promoter”. Free Radic. Biol. Med. 37 (8): 1231ā43. doi:10.1016/j.freeradbiomed.2004.06.042. PMIDĀ 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): 2121ā7. doi:10.1101/gr.2596504. PMCĀ 528928. PMIDĀ 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): 223ā30. doi:10.1016/j.bbrc.2005.06.073. PMIDĀ 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): 332ā8. doi:10.1016/j.bbrc.2005.08.081. PMIDĀ 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): 1173ā8. doi:10.1038/nature04209. PMIDĀ 16189514.
