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Identification
HMDB Protein ID HMDBP00138
Secondary Accession Numbers
  • 5370
Name Ribosyldihydronicotinamide dehydrogenase [quinone]
Synonyms
  1. NRH dehydrogenase [quinone] 2
  2. NRH:quinone oxidoreductase 2
  3. QR2
  4. Quinone reductase 2
Gene Name NQO2
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 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.
Pathways Not Available
Reactions
1-(beta-D-Ribofuranosyl)-1,4-dihydronicotinamide + a quinone → 1-(beta-D-ribofuranosyl)nicotinamide + a hydroquinone details
GO Classification
Cellular Component
cytoplasm
nucleus
Function
binding
catalytic activity
electron carrier activity
coenzyme binding
cofactor binding
oxidoreductase activity
Molecular Function
electron carrier activity
metal ion binding
dihydronicotinamide riboside quinone reductase activity
NADPH dehydrogenase (quinone) activity
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 6
Locus 6p25.2
SNPs NQO2
Gene Sequence
>696 bp
ATGGCAGGTAAGAAAGTACTCATTGTCTATGCACACCAGGAACCCAAGTCTTTCAACGGA
TCCTTGAAGAATGTGGCTGTAGATGAACTGAGCAGGCAGGGCTGCACCGTCACAGTGTCT
GATTTGTATGCCATGAACTTTGAGCCGAGGGCCACAGACAAAGATATCACTGGTACTCTT
TCTAATCCTGAGGTTTTCAATTATGGAGTGGAAACCCACGAAGCCTACAAGCAAAGGTCT
CTGGCTAGCGACATCACTGATGAGCAGAAAAAGGTTCGGGAGGCTGACCTAGTGATATTT
CAGTTCCCGCTGTACTGGTTCAGCGTGCCGGCCATCCTGAAGGGCTGGATGGATAGGGTG
CTGTGCCAGGGCTTTGCCTTTGACATCCCAGGATTCTACGATTCCGGTTTGCTCCAGGGT
AAACTAGCGCTCCTTTCCGTAACCACGGGAGGCACGGCCGAGATGTACACGAAGACAGGA
GTCAATGGAGATTCTCGATACTTCCTGTGGCCACTCCAGCATGGCACATTACACTTCTGT
GGATTTAAAGTCCTTGCCCCTCAGATCAGCTTTGCTCCTGAAATTGCATCCGAAGAAGAA
AGAAAGGGGATGGTGGCTGCGTGGTCCCAGAGGCTGCAGACCATCTGGAAGGAAGAGCCC
ATCCCCTGCACAGCCCACTGGCACTTCGGGCAATAA
Protein Properties
Number of Residues 231
Molecular Weight 25918.4
Theoretical pI 6.289
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Ribosyldihydronicotinamide dehydrogenase [quinone]
MAGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNFEPRATDKDITGTL
SNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRV
LCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGDSRYFLWPLQHGTLHFC
GFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ
GenBank ID Protein Not Available
UniProtKB/Swiss-Prot ID P16083
UniProtKB/Swiss-Prot Entry Name NQO2_HUMAN
PDB IDs
GenBank Gene ID J02888
GeneCard ID NQO2
GenAtlas ID NQO2
HGNC ID HGNC:7856
References
General References
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  4. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
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  6. 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 ]
  7. 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 ]
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  9. 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 ]
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  11. 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 ]
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  13. 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 ]
  14. 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 ]
  15. 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 ]
  16. 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 ]