Ribosyldihydronicotinamide dehydrogenase [quinone]

Details

Name
Ribosyldihydronicotinamide dehydrogenase [quinone]
Synonyms
  • 1.10.5.1
  • NMOR2
  • NRH dehydrogenase [quinone] 2
  • NRH:quinone oxidoreductase 2
  • QR2
  • Quinone reductase 2
Gene Name
NQO2
Organism
Humans
Amino acid sequence
>lcl|BSEQ0010014|Ribosyldihydronicotinamide dehydrogenase [quinone]
MAGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLEPRATDKDITGTL
SNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRV
LCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGDSRYFLWPLQHGTLHFC
GFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ
Number of residues
231
Molecular Weight
25918.4
Theoretical pI
6.24
GO Classification
Functions
electron carrier activity / metal ion binding / NADPH dehydrogenase (quinone) activity
Processes
memory
Components
cytoplasm / extracellular exosome / nucleoplasm
General Function
Nadph dehydrogenase (quinone) activity
Specific Function
The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0010015|Ribosyldihydronicotinamide dehydrogenase [quinone] (NQO2)
ATGGCAGGTAAGAAAGTACTCATTGTCTATGCACACCAGGAACCCAAGTCTTTCAACGGA
TCCTTGAAGAATGTGGCTGTAGATGAACTGAGCAGGCAGGGCTGCACCGTCACAGTGTCT
GATTTGTATGCCATGAACCTTGAGCCGAGGGCCACAGACAAAGATATCACTGGTACTCTT
TCTAATCCTGAGGTTTTCAATTATGGAGTGGAAACCCACGAAGCCTACAAGCAAAGGTCT
CTGGCTAGCGACATCACTGATGAGCAGAAAAAGGTTCGGGAGGCTGACCTAGTGATATTT
CAGTTCCCGCTGTACTGGTTCAGCGTGCCAGCCATCCTGAAGGGCTGGATGGATAGGGTG
CTGTGCCAGGGCTTTGCCTTTGACATCCCAGGATTCTACGATTCCGGTTTGCTCCAGGGT
AAACTAGCGCTCCTTTCCGTAACCACGGGAGGCACGGCCGAGATGTACACGAAGACAGGA
GTCAATGGAGATTCTCGATACTTCCTGTGGCCACTCCAGCATGGCACATTACACTTCTGT
GGATTTAAAGTCCTTGCCCCTCAGATCAGCTTTGCTCCTGAAATTGCATCCGAAGAAGAA
AGAAAGGGGATGGTGGCTGCGTGGTCCCAGAGGCTGCAGACCATCTGGAAGGAAGAGCCC
ATCCCCTGCACAGCCCACTGGCACTTCGGGCAATAA
Chromosome Location
6
Locus
6pter-q12
External Identifiers
ResourceLink
UniProtKB IDP16083
UniProtKB Entry NameNQO2_HUMAN
GenBank Protein ID190818
GenBank Gene IDJ02888
GenAtlas IDNQO2
HGNC IDHGNC:7856
General References
  1. Jaiswal AK, Burnett P, Adesnik M, McBride OW: 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. 1990 Feb 20;29(7):1899-906. [PubMed:1691923]
  2. Jaiswal AK: Human NAD(P)H:quinone oxidoreductase2. Gene structure, activity, and tissue-specific expression. J Biol Chem. 1994 May 20;269(20):14502-8. [PubMed:8182056]
  3. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039]
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  6. Wu K, Knox R, Sun XZ, Joseph P, Jaiswal AK, Zhang D, Deng PS, Chen S: Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase. Arch Biochem Biophys. 1997 Nov 15;347(2):221-8. [PubMed:9367528]
  7. Zhao Q, Yang XL, Holtzclaw WD, Talalay P: 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. 1997 Mar 4;94(5):1669-74. [PubMed:9050836]
  8. Kwiek JJ, Haystead TA, Rudolph J: Kinetic mechanism of quinone oxidoreductase 2 and its inhibition by the antimalarial quinolines. Biochemistry. 2004 Apr 20;43(15):4538-47. [PubMed:15078100]
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  11. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [PubMed:24275569]
  12. Foster CE, Bianchet MA, Talalay P, Zhao Q, Amzel LM: Crystal structure of human quinone reductase type 2, a metalloflavoprotein. Biochemistry. 1999 Aug 3;38(31):9881-6. [PubMed:10433694]
  13. Buryanovskyy L, Fu Y, Boyd M, Ma Y, Hsieh TC, Wu JM, Zhang Z: Crystal structure of quinone reductase 2 in complex with resveratrol. Biochemistry. 2004 Sep 14;43(36):11417-26. [PubMed:15350128]
  14. Fu Y, Buryanovskyy L, Zhang Z: Crystal structure of quinone reductase 2 in complex with cancer prodrug CB1954. Biochem Biophys Res Commun. 2005 Oct 14;336(1):332-8. [PubMed:16129418]
  15. Calamini B, Santarsiero BD, Boutin JA, Mesecar AD: Kinetic, thermodynamic and X-ray structural insights into the interaction of melatonin and analogues with quinone reductase 2. Biochem J. 2008 Jul 1;413(1):81-91. doi: 10.1042/BJ20071373. [PubMed:18254726]
  16. Fu Y, Buryanovskyy L, Zhang Z: Quinone reductase 2 is a catechol quinone reductase. J Biol Chem. 2008 Aug 29;283(35):23829-35. doi: 10.1074/jbc.M801371200. Epub 2008 Jun 24. [PubMed:18579530]
  17. Winger JA, Hantschel O, Superti-Furga G, Kuriyan J: The structure of the leukemia drug imatinib bound to human quinone reductase 2 (NQO2). BMC Struct Biol. 2009 Feb 24;9:7. doi: 10.1186/1472-6807-9-7. [PubMed:19236722]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00157NADHapproved, nutraceuticalunknownDetails
DB02709Resveratrolapproved, experimental, investigationalunknownDetails
DB03147Flavin adenine dinucleotideapprovedunknownDetails
DB00170Menadioneapproved, nutraceuticalunknownDetails
DB01065Melatoninapproved, nutraceutical, vet_approvedunknownDetails
DB07339(3S)-3-hydroxy-1-methyl-2,3-dihydro-1H-indole-5,6-dioneexperimentalunknownDetails
DB04253TretazicarinvestigationalunknownDetails
DB0354110-Propargyl-5,8-Dideazafolic AcidexperimentalunknownDetails
DB08190N-[2-(2-iodo-5-methoxy-1H-indol-3-yl)ethyl]acetamideexperimentalunknownDetails
DB082285,8-dimethoxy-1,4-dimethylquinolin-2(1H)-oneexperimentalunknownDetails
DB087446-methoxy-9-methyl[1,3]dioxolo[4,5-h]quinolin-8(9H)-oneexperimentalunknownDetails
DB01087PrimaquineapprovedunknowninhibitorDetails
DB06695Dabigatran etexilateapprovedunknowninhibitorDetails
DB04216Quercetinexperimental, investigationalunknowninhibitorDetails