메뉴 건너뛰기




Volumn 29, Issue 3-4, 2000, Pages 276-284

Structure-function studies of DT-diaphorase (NQO1) and NRH:quinone oxidoreductase (NQO2)

Author keywords

CB1954; DT diaphorase; Free radicals; NQO1; NQO2; Prodrug; Site directed mutagenesis

Indexed keywords

OXIDOREDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE);

EID: 0033805383     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(00)00308-7     Document Type: Article
Times cited : (93)

References (53)
  • 1
    • 0000964637 scopus 로고
    • Soluble diaphorase in animal tissues
    • Ernster L., Navazioi F. Soluble diaphorase in animal tissues. Acta Chem. Scand. 12:1958;595.
    • (1958) Acta Chem. Scand. , vol.12 , pp. 595
    • Ernster, L.1    Navazioi, F.2
  • 2
    • 0003123510 scopus 로고
    • Purification and some properties of a highly dicumarol-sensitive liver diaphorase
    • Ernster L., Liunggren M., Danielson L. Purification and some properties of a highly dicumarol-sensitive liver diaphorase. Biochem. Biophys. Res. Commun. 2:1960;88-92.
    • (1960) Biochem. Biophys. Res. Commun. , vol.2 , pp. 88-92
    • Ernster, L.1    Liunggren, M.2    Danielson, L.3
  • 3
    • 0025018844 scopus 로고
    • 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
    • Jaiswal A.K., Burnett P., Adesnik M., McBride O.W. 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. 29:1990;1899-1906.
    • (1990) Biochemistry , vol.29 , pp. 1899-1906
    • Jaiswal, A.K.1    Burnett, P.2    Adesnik, M.3    McBride, O.W.4
  • 4
    • 0031573462 scopus 로고    scopus 로고
    • Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase
    • Wu K., Knox R., Sun X.Z., Joseph P., Jaiswal A.K., Zhang D., Deng P.S.-K., Chen S. Catalytic properties of NAD(P)H:quinone oxidoreductase-2 (NQO2), a dihydronicotinamide riboside dependent oxidoreductase. Arch. Biochem. Biophys. 347:1997;221-228.
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 221-228
    • Wu, K.1    Knox, R.2    Sun, X.Z.3    Joseph, P.4    Jaiswal, A.K.5    Zhang, D.6    Deng, P.S.-K.7    Chen, S.8
  • 5
    • 0000874497 scopus 로고
    • Purification and properties of a flavoprotein catalyzing the oxidation of reduced ribosyl nicotinamide
    • Liao S., Dulaney J.T., Williams-Ashman H.G. Purification and properties of a flavoprotein catalyzing the oxidation of reduced ribosyl nicotinamide. J. Biol. Chem. 237:1962;2981-2987.
    • (1962) J. Biol. Chem. , vol.237 , pp. 2981-2987
    • Liao, S.1    Dulaney, J.T.2    Williams-Ashman, H.G.3
  • 7
    • 0031026290 scopus 로고    scopus 로고
    • Molecular basis of the catalytic differences among DT-diaphorase of human, rat, and mouse
    • Chen S., Knox R., Wu K., Deng P.S.-K., Zhou D., Bianchet M.A., Amzel L.M. Molecular basis of the catalytic differences among DT-diaphorase of human, rat, and mouse. J. Biol. Chem. 272:1997;1437-1439.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1437-1439
    • Chen, S.1    Knox, R.2    Wu, K.3    Deng, P.S.-K.4    Zhou, D.5    Bianchet, M.A.6    Amzel, L.M.7
  • 8
    • 0032793633 scopus 로고    scopus 로고
    • Molecular characterization of binding of substrates and inhibitors to DT-diaphorase: Combined approach involving site-directed mutagenesis, inhibitor-binding analysis, and computer modeling
    • Chen S., Wu K., Zhang D., Sherman M., Knox R., Yang C.S. Molecular characterization of binding of substrates and inhibitors to DT-diaphorase combined approach involving site-directed mutagenesis, inhibitor-binding analysis, and computer modeling . Mol. Pharmacol. 56:1999;272-278.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 272-278
    • Chen, S.1    Wu, K.2    Zhang, D.3    Sherman, M.4    Knox, R.5    Yang, C.S.6
  • 9
    • 0002117840 scopus 로고
    • DT diaphorase: A historical review
    • Ernster L. DT diaphorase a historical review . Chemica Scripta. 27A:1987;1-13.
    • (1987) Chemica Scripta , vol.27 , pp. 1-13
    • Ernster, L.1
  • 10
    • 0022977882 scopus 로고
    • NAD(P)H:menadione oxidoreductase: Novel purification of enzyme, cDNA, and complete amino acid sequence, and gene regulation
    • Robertson J.A., Chen H.-C., Nebert D.W. NAD(P)H:menadione oxidoreductase novel purification of enzyme, cDNA, and complete amino acid sequence, and gene regulation . J. Biol. Chem. 261:1986;15794-15799.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15794-15799
    • Robertson, J.A.1    Chen, H.-C.2    Nebert, D.W.3
  • 11
    • 0023134930 scopus 로고
    • Rat liver NAD(P)H:quinone reductase nucleotide sequence analysis of a quinone reductase cDNA clone and prediction of the amino acid sequence of the corresponding protein
    • Bayney R.M., Rodkey J.A., Bennett C.D., Lu A.R.H., Pickett C.B. Rat liver NAD(P)H:quinone reductase nucleotide sequence analysis of a quinone reductase cDNA clone and prediction of the amino acid sequence of the corresponding protein. J. Biol. Chem. 262:1987;572-575.
    • (1987) J. Biol. Chem. , vol.262 , pp. 572-575
    • Bayney, R.M.1    Rodkey, J.A.2    Bennett, C.D.3    Lu, A.R.H.4    Pickett, C.B.5
  • 12
    • 0023758288 scopus 로고
    • Structure-function relationship of NAD(P)H:quinone reductase: Characterization of NH2-terminal blocking group and essential tyrosine and lysine residues
    • Haniu M., Yuan H., Chen S., Iyanagi T., Lee T.D., Shively J.E. Structure-function relationship of NAD(P)H:quinone reductase characterization of NH2-terminal blocking group and essential tyrosine and lysine residues . Biochemistry. 27:1988;6877-6883.
    • (1988) Biochemistry , vol.27 , pp. 6877-6883
    • Haniu, M.1    Yuan, H.2    Chen, S.3    Iyanagi, T.4    Lee, T.D.5    Shively, J.E.6
  • 13
    • 0023724493 scopus 로고
    • Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase: CDNA sequence and localization of gene to chromosome 16
    • Jaiswal A.K., McBride O.W., Adesnik M., Nebert D.W. Human dioxin-inducible cytosolic NAD(P)H:menadione oxidoreductase cDNA sequence and localization of gene to chromosome 16 . J. Biol. Chem. 263:1988;13572-13578.
    • (1988) J. Biol. Chem. , vol.263 , pp. 13572-13578
    • Jaiswal, A.K.1    McBride, O.W.2    Adesnik, M.3    Nebert, D.W.4
  • 14
    • 0028031271 scopus 로고
    • Mouse liver NAD(P)H:quinone acceptor oxidoreductase: Protein sequence analysis by tandem mass spectrometry, cDNA cloning, expression in Escherichia coli, and enzyme activity analysis
    • Chen S., Clarke P.E., Martino P.A., Deng P.S.K., Yeh C.-H., Lee T.D., Prochaska H.J., Talalay P. Mouse liver NAD(P)H:quinone acceptor oxidoreductase protein sequence analysis by tandem mass spectrometry, cDNA cloning, expression in Escherichia coli, and enzyme activity analysis . Protein Sci. 3:1994;1296-1304.
    • (1994) Protein Sci , vol.3 , pp. 1296-1304
    • Chen, S.1    Clarke, P.E.2    Martino, P.A.3    Deng, P.S.K.4    Yeh, C.-H.5    Lee, T.D.6    Prochaska, H.J.7    Talalay, P.8
  • 15
    • 0026762694 scopus 로고
    • Expression of rat liver NAD(P)H:quinone acceptor oxidoreductase in E. coli and in vitro mutagenesis at Arg-177
    • Chen H.H., Ma J.X., Forrest G.L., Deng P.S.K., Martino P., Lee T.D., Chen S. Expression of rat liver NAD(P)H:quinone acceptor oxidoreductase in E. coli and in vitro mutagenesis at Arg-177. Biochem. J. 284:1992;855-860.
    • (1992) Biochem. J. , vol.284 , pp. 855-860
    • Chen, H.H.1    Ma, J.X.2    Forrest, G.L.3    Deng, P.S.K.4    Martino, P.5    Lee, T.D.6    Chen, S.7
  • 16
    • 0024364670 scopus 로고
    • Reaction of rat liver DT-diaphorase (NAD(P)H:quinone acceptor reductase) with 5′-[p-(fluorosulfonyl)benzoyl]-adenosine
    • Liu X.-F., Yuan H., Haniu M., Iyanagi T., Shively J.E., Chen S. Reaction of rat liver DT-diaphorase (NAD(P)H:quinone acceptor reductase) with 5′-[p-(fluorosulfonyl)benzoyl]-adenosine. Mol. Pharmacol. 35:1989;818-822.
    • (1989) Mol. Pharmacol. , vol.35 , pp. 818-822
    • Liu, X.-F.1    Yuan, H.2    Haniu, M.3    Iyanagi, T.4    Shively, J.E.5    Chen, S.6
  • 19
    • 0026717638 scopus 로고
    • Site-directed mutagenesis of rat liver NAD(P)H:quinone oxidoreductase: Roles of lysine 76 and cysteine 179
    • Ma Q., Cui K., Wang R.W., Lu A.Y.H., Yang C.S. Site-directed mutagenesis of rat liver NAD(P)H:quinone oxidoreductase roles of lysine 76 and cysteine 179 . Arch. Biochem. Biophys. 294:1992;434-439.
    • (1992) Arch. Biochem. Biophys. , vol.294 , pp. 434-439
    • Ma, Q.1    Cui, K.2    Wang, R.W.3    Lu, A.Y.H.4    Yang, C.S.5
  • 20
    • 0026499189 scopus 로고
    • Identification of a glycine-rich sequence as an NAD(P)H-binding site and tyrosine 128 as a dicoumarol-binding site in rat liver NAD(P)H:quinone oxidoreductase by site-directed mutagenesis
    • Ma Q., Cui K., Xiao F., Lu A.Y.H., Yang C.S. Identification of a glycine-rich sequence as an NAD(P)H-binding site and tyrosine 128 as a dicoumarol-binding site in rat liver NAD(P)H:quinone oxidoreductase by site-directed mutagenesis. J. Biol. Chem. 267:1992;22298-22304.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22298-22304
    • Ma, Q.1    Cui, K.2    Xiao, F.3    Lu, A.Y.H.4    Yang, C.S.5
  • 21
    • 0028882146 scopus 로고
    • Roles of histidine-194, aspartate-163, and a glycine-rich sequence of NAD(P)H:quinone oxidoreductase in the interaction with nicotinamide coenzymes
    • Cui K., Ma Q., Lu A.Y.H., Yang C.S. Roles of histidine-194, aspartate-163, and a glycine-rich sequence of NAD(P)H:quinone oxidoreductase in the interaction with nicotinamide coenzymes. Arch. Biochem. Biophys. 323:1995;265-273.
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 265-273
    • Cui, K.1    Ma, Q.2    Lu, A.Y.H.3    Yang, C.S.4
  • 22
    • 0029068515 scopus 로고
    • The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy: Mechanism of the two-electron reaction
    • Li R., Bianchet M.A., Talalay P., Amzel L.M. The three-dimensional structure of NAD(P)H:quinone reductase, a flavoprotein involved in cancer chemoprotection and chemotherapy mechanism of the two-electron reaction . Proc. Natl. Acad. Sci. USA. 92:1995;8846-8850.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8846-8850
    • Li, R.1    Bianchet, M.A.2    Talalay, P.3    Amzel, L.M.4
  • 23
    • 0034724218 scopus 로고    scopus 로고
    • Structures of recombinant human and mouse NAD(P)H:quinone oxidoreductases: Species comparison and structural changes with substrate binding and release
    • Faig M., Bianchet M.A., Talalay P., Chen S., Winski S., Ross D., Amzel L.M. 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. USA. 97:2000;3177-3182.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3177-3182
    • Faig, M.1    Bianchet, M.A.2    Talalay, P.3    Chen, S.4    Winski, S.5    Ross, D.6    Amzel, L.M.7
  • 24
    • 0017839373 scopus 로고
    • NAD(P)H dehydrogenase and its role in the vitamin K (2-methyl-3-phytyl-1,4-naphthaquinone)-dependent carboxylation reaction
    • Wallin R., Gerhardt O., Prydz H. NAD(P)H dehydrogenase and its role in the vitamin K (2-methyl-3-phytyl-1,4-naphthaquinone)-dependent carboxylation reaction. Biochem. J. 169:1978;95-101.
    • (1978) Biochem. J. , vol.169 , pp. 95-101
    • Wallin, R.1    Gerhardt, O.2    Prydz, H.3
  • 25
    • 0011945019 scopus 로고
    • DT-diaphorase properties, reaction mechanism, metabolic function. A progress report
    • T.E. King, H.S. Mason, & M. Morrison. New York: Pergamon Press
    • Lind C., Hochstein P., Ernster L. DT-diaphorase properties, reaction mechanism, metabolic function. A progress report. King T.E., Mason H.S., Morrison M. Symposium on oxidases and related redox systems. 1979;321-347 Pergamon Press, New York.
    • (1979) Symposium on Oxidases and Related Redox Systems , pp. 321-347
    • Lind, C.1    Hochstein, P.2    Ernster, L.3
  • 26
    • 0016697619 scopus 로고
    • Studies on the reaction mechanism of DT-diaphorase. Action of dead-end inhibitors and effects of phospholipids
    • Hollander P.M., Ernster L. Studies on the reaction mechanism of DT-diaphorase. Action of dead-end inhibitors and effects of phospholipids. Arch. Biochem. Biophys. 169:1975;560-567.
    • (1975) Arch. Biochem. Biophys. , vol.169 , pp. 560-567
    • Hollander, P.M.1    Ernster, L.2
  • 27
    • 0025280109 scopus 로고
    • Inhibition of rat liver DT-diaphorase (NAD(P)H:quinone acceptor reductase) by flavonoids isolated from the Chinese herb, Scutellariae Radix (Huang Qin)
    • Liu X.-F., Liu M.-L., Iyanagi T., Legesse K., Lee T.D., Chen S. Inhibition of rat liver DT-diaphorase (NAD(P)H:quinone acceptor reductase) by flavonoids isolated from the Chinese herb, Scutellariae Radix (Huang Qin). Mol. Pharmacol. 37:1990;911-915.
    • (1990) Mol. Pharmacol. , vol.37 , pp. 911-915
    • Liu, X.-F.1    Liu, M.-L.2    Iyanagi, T.3    Legesse, K.4    Lee, T.D.5    Chen, S.6
  • 28
    • 0025258497 scopus 로고
    • Metabolism of diaziquone by NAD(P)H:quinone acceptor oxidoreductase (DT-diaphorase): Role in diaziquone-induced DNA damage and cytotoxicity in human colon carcinoma cells
    • Siegel D., Gibson N.W., Preusch P.C., Ross D. Metabolism of diaziquone by NAD(P)H:quinone acceptor oxidoreductase (DT-diaphorase) role in diaziquone-induced DNA damage and cytotoxicity in human colon carcinoma cells . Cancer Res. 50:1990;7293-7300.
    • (1990) Cancer Res , vol.50 , pp. 7293-7300
    • Siegel, D.1    Gibson, N.W.2    Preusch, P.C.3    Ross, D.4
  • 29
    • 0025688249 scopus 로고
    • Metabolism of mitomycin C by DT-diaphorase: Role in mitomycin C-induced DNA damage and cytotoxicity in human colon carcinoma cells
    • Siegel D., Gibson N.W., Preusch P.C., Ross D. Metabolism of mitomycin C by DT-diaphorase role in mitomycin C-induced DNA damage and cytotoxicity in human colon carcinoma cells . Cancer Res. 50:1990;7483-7489.
    • (1990) Cancer Res , vol.50 , pp. 7483-7489
    • Siegel, D.1    Gibson, N.W.2    Preusch, P.C.3    Ross, D.4
  • 30
    • 0025893246 scopus 로고
    • The role of NAD(P)H:quinone reductase (EC 1. 6. 99. 2, DT-diaphorase) in the reductive bioactivation of the novel indoloquinone antitumor agent EO9
    • Walton M.I., Smith P.J., Workman P. The role of NAD(P)H:quinone reductase (EC 1. 6. 99. 2, DT-diaphorase) in the reductive bioactivation of the novel indoloquinone antitumor agent EO9. Cancer Commun. 3:1991;199-206.
    • (1991) Cancer Commun , vol.3 , pp. 199-206
    • Walton, M.I.1    Smith, P.J.2    Workman, P.3
  • 31
    • 0026034848 scopus 로고
    • The differences in kinetics of rat and human DT diaphorase result in a differential sensitivity of derived cell lines to CB 1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide)
    • Boland M.P., Knox R.J., Roberts J.J. The differences in kinetics of rat and human DT diaphorase result in a differential sensitivity of derived cell lines to CB 1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). Biochem. Pharmacol. 41:1991;867-875.
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 867-875
    • Boland, M.P.1    Knox, R.J.2    Roberts, J.J.3
  • 32
    • 0015451983 scopus 로고
    • Potential bioreductive alkylating agents. 1. Benzoquinone derivatives
    • Lin A.J., Cosby L.A., Shansky C.W., Sartorelli A.C. Potential bioreductive alkylating agents. 1. Benzoquinone derivatives. J. Med. Chem. 15:1972;1247-1252.
    • (1972) J. Med. Chem. , vol.15 , pp. 1247-1252
    • Lin, A.J.1    Cosby, L.A.2    Shansky, C.W.3    Sartorelli, A.C.4
  • 33
    • 0026505943 scopus 로고
    • NAD(P):quinone oxidoreductase gene expression in human colon carcinoma cells: Characterization of a mutation which modulates DT-diaphorase activity and mitomycin sensitivity
    • Traver R.D., Horikoshi T., Danenberg K.D., Stadlbauer T.H., Danenberg P.V., Ross D., Gibson N.W. NAD(P):quinone oxidoreductase gene expression in human colon carcinoma cells characterization of a mutation which modulates DT-diaphorase activity and mitomycin sensitivity . Cancer Res. 52:1992;797-802.
    • (1992) Cancer Res , vol.52 , pp. 797-802
    • Traver, R.D.1    Horikoshi, T.2    Danenberg, K.D.3    Stadlbauer, T.H.4    Danenberg, P.V.5    Ross, D.6    Gibson, N.W.7
  • 34
    • 0028833858 scopus 로고
    • NAD(P)H:quinone oxidoreductase expression and mitomycin C resistance developed by human colon cancer HCT 116 cells
    • Pan S.S., Forrest G.L., Akman S.A., Hu L.T. NAD(P)H:quinone oxidoreductase expression and mitomycin C resistance developed by human colon cancer HCT 116 cells. . Cancer Res. 55:1995;330-335.
    • (1995) . Cancer Res. , vol.55 , pp. 330-335
    • Pan, S.S.1    Forrest, G.L.2    Akman, S.A.3    Hu, L.T.4
  • 35
    • 0021345793 scopus 로고
    • Reductive activation of mitomycin C and mitomycin C metabolites catalyzed by NADPH-cytochrome P450 reductase and xanthine oxidase
    • Bachur N.R., Gordon S.L., Gee M.V., Kon H. Reductive activation of mitomycin C and mitomycin C metabolites catalyzed by NADPH-cytochrome P450 reductase and xanthine oxidase. J. Biol. Chem. 259:1979;959-966.
    • (1979) J. Biol. Chem. , vol.259 , pp. 959-966
    • Bachur, N.R.1    Gordon, S.L.2    Gee, M.V.3    Kon, H.4
  • 36
    • 0021345793 scopus 로고
    • Reductive activation of mitomycin C and mitomycin C metabolites catalyzed by NADPH-cytochrome P450 reductase and xanthine oxidase
    • Pan S.S., Andrews P.A., Glover C.J. Reductive activation of mitomycin C and mitomycin C metabolites catalyzed by NADPH-cytochrome P450 reductase and xanthine oxidase. J. Biol. Chem. 259:1984;959-966.
    • (1984) J. Biol. Chem. , vol.259 , pp. 959-966
    • Pan, S.S.1    Andrews, P.A.2    Glover, C.J.3
  • 37
    • 0026032132 scopus 로고
    • Studies on the mechanism of resistance to mitomycin C and porfiromycin in a human cell strain derived from a cancer-prone individual
    • Marshall R.S., Paterson M.C., Rauth A.M. Studies on the mechanism of resistance to mitomycin C and porfiromycin in a human cell strain derived from a cancer-prone individual. Biochem. Pharmacol. 41:1991;1351-1360.
    • (1991) Biochem. Pharmacol. , vol.41 , pp. 1351-1360
    • Marshall, R.S.1    Paterson, M.C.2    Rauth, A.M.3
  • 38
    • 0025797202 scopus 로고
    • Chinese hamster ovary cell lines resistant to mitomycin C under aerobic but not hypoxic conditions are deficient in DT-diaphorase
    • Dulhanty A.M., Whitmore G.F. Chinese hamster ovary cell lines resistant to mitomycin C under aerobic but not hypoxic conditions are deficient in DT-diaphorase. . Cancer Res. 51:1991;1860-1865.
    • (1991) . Cancer Res. , vol.51 , pp. 1860-1865
    • Dulhanty, A.M.1    Whitmore, G.F.2
  • 39
    • 0027182862 scopus 로고
    • The bioactivation of CB 1954 and its use as a prodrug in antibody-directed enzyme prodrug therapy (ADEPT)
    • Knox R.J., Friedlos F., Boland M.P. The bioactivation of CB 1954 and its use as a prodrug in antibody-directed enzyme prodrug therapy (ADEPT). Cancer Metastasis Rev. 12:1993;195-212.
    • (1993) Cancer Metastasis Rev , vol.12 , pp. 195-212
    • Knox, R.J.1    Friedlos, F.2    Boland, M.P.3
  • 40
    • 0024205344 scopus 로고
    • The nitroreductase enzyme in Walker cells that activates 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954) to 5-(aziridin-1-yl)-4-hydroxylamino-2-nitrobenzamide is a form of NAD(P)H dehydrogenase (quinone) (EC 1. 6. 99. 2)
    • Knox R.J., Boland M.P., Friedlos F., Coles B., Southan C., Roberts J.J. The nitroreductase enzyme in Walker cells that activates 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954) to 5-(aziridin-1-yl)-4-hydroxylamino-2-nitrobenzamide is a form of NAD(P)H dehydrogenase (quinone) (EC 1. 6. 99. 2). Biochem. Pharmacol. 37:1988;4671-4677.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 4671-4677
    • Knox, R.J.1    Boland, M.P.2    Friedlos, F.3    Coles, B.4    Southan, C.5    Roberts, J.J.6
  • 41
    • 0024209370 scopus 로고
    • A new cytotoxic, DNA interstrand crosslinking agent, 5-(aziridin-1-yl)-4-hydroxylamino-2-nitrobenzamide, is formed from 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954) by a nitroreductase enzyme in Walker carcinoma cells
    • Knox R.J., Friedlos F., Jarman M., Robert J.J. A new cytotoxic, DNA interstrand crosslinking agent, 5-(aziridin-1-yl)-4-hydroxylamino-2-nitrobenzamide, is formed from 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB 1954) by a nitroreductase enzyme in Walker carcinoma cells. Biochem. Pharmacol. 37:1988;4661-4669.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 4661-4669
    • Knox, R.J.1    Friedlos, F.2    Jarman, M.3    Robert, J.J.4
  • 42
    • 0026075733 scopus 로고
    • Bioactivation of CB 1954: Reaction of the active 4-hydroxylamino derivative with thioesters to form the ultimate DNA-DNA interstrand cross-linking species
    • Knox R.J., Friedlos F., Marchbank T., Robert J.J. Bioactivation of CB 1954 reaction of the active 4-hydroxylamino derivative with thioesters to form the ultimate DNA-DNA interstrand cross-linking species . Biochem. Pharmacol. 42:1991;1691-1697.
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 1691-1697
    • Knox, R.J.1    Friedlos, F.2    Marchbank, T.3    Robert, J.J.4
  • 43
    • 0019142866 scopus 로고
    • Increase of NAD(P)H:quinone reductase by dietary antioxidants: Possible role in protection against carcinogenesis and toxicity
    • Benson A.M., Hunkeler M.J., Talalay P. Increase of NAD(P)H:quinone reductase by dietary antioxidants possible role in protection against carcinogenesis and toxicity . Proc. Natl. Acad. Sci. USA. 77:1980;5216-5220.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5216-5220
    • Benson, A.M.1    Hunkeler, M.J.2    Talalay, P.3
  • 44
    • 0014842505 scopus 로고
    • One-electron-transfer reactions in biochemical systems. V. Difference in the mechanism of quinone reductase by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase)
    • Iyanagi T., Yamazaki I. One-electron-transfer reactions in biochemical systems. V. Difference in the mechanism of quinone reductase by the NADH dehydrogenase and the NAD(P)H dehydrogenase (DT-diaphorase). Biochim. Biophys. Acta. 216:1970;282-294.
    • (1970) Biochim. Biophys. Acta , vol.216 , pp. 282-294
    • Iyanagi, T.1    Yamazaki, I.2
  • 45
    • 0002783125 scopus 로고
    • On the mechanisms of one- And two-electron transfer by flavin enzymes
    • Iyanagi T. On the mechanisms of one- and two-electron transfer by flavin enzymes. Chemica Scripta. 27A:1987;31-36.
    • (1987) Chemica Scripta , vol.27 , pp. 31-36
    • Iyanagi, T.1
  • 46
    • 0028893931 scopus 로고
    • DT-diaphorase. Redox Potential, steady-state, and rapid reaction studies
    • Tedeschi G., Chen S., Massey V. DT-diaphorase. Redox Potential, steady-state, and rapid reaction studies. J. Biol. Chem. 270:1995;1198-1204.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1198-1204
    • Tedeschi, G.1    Chen, S.2    Massey, V.3
  • 47
    • 0028847678 scopus 로고
    • Active site studies of DT-diaphorase employing artifical flavins
    • Tedeschi G., Chen S., Massey V. Active site studies of DT-diaphorase employing artifical flavins. J. Biol. Chem. 270:1995;2512-2516.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2512-2516
    • Tedeschi, G.1    Chen, S.2    Massey, V.3
  • 48
    • 0029151835 scopus 로고
    • Presence of a heterozygous substitution and its relationship to DT-diaphorase activity
    • Kuehl B.L., Paterson J.W.E., Peacock J.W., Paterson M.C., Rauth A.M. Presence of a heterozygous substitution and its relationship to DT-diaphorase activity. Br. J. Cancer. 72:1995;555-561.
    • (1995) Br. J. Cancer , vol.72 , pp. 555-561
    • Kuehl, B.L.1    Paterson, J.W.E.2    Peacock, J.W.3    Paterson, M.C.4    Rauth, A.M.5
  • 50
    • 0000962684 scopus 로고    scopus 로고
    • Catalytic properties of a naturally occurring mutant of human NAD(P)H:quinone acceptor oxidoreductase (DT-diaphorase), Pro-187 to Ser
    • K. Yagi. Basel, Switzerland: Karger
    • Wu K., Deng P.S.-K., Chen S. Catalytic properties of a naturally occurring mutant of human NAD(P)H:quinone acceptor oxidoreductase (DT-diaphorase), Pro-187 to Ser. Yagi K. Pathophysiology of lipid peroxides and related free radicals. 1998;135-148 Karger, Basel, Switzerland.
    • (1998) Pathophysiology of Lipid Peroxides and Related Free Radicals , pp. 135-148
    • Wu, K.1    Deng, P.S.-K.2    Chen, S.3
  • 51
    • 0029083939 scopus 로고
    • Involvement of Lys-113 in the binding of the FAD prosthetic group of NAD(P)H:quinone acceptor oxidoreductase
    • Tedeschi G., Deng P.S.-K., Chen H.H., Massey V., Forrest G.L., Chen S. Involvement of Lys-113 in the binding of the FAD prosthetic group of NAD(P)H:quinone acceptor oxidoreductase. Arch. Biochem. Biophys. 321:1995;76-82.
    • (1995) Arch. Biochem. Biophys. , vol.321 , pp. 76-82
    • Tedeschi, G.1    Deng, P.S.-K.2    Chen, H.H.3    Massey, V.4    Forrest, G.L.5    Chen, S.6
  • 52
    • 0029058447 scopus 로고
    • An alternatively spliced form of NQO1 (DT-diaphorase) messenger RNA lackingthe putative quinone substrate binding site is present in human normal and tumor tissues
    • Gasdaska P.Y., Fisher H., Powis G. An alternatively spliced form of NQO1 (DT-diaphorase) messenger RNA lackingthe putative quinone substrate binding site is present in human normal and tumor tissues. Cancer Res. 55:1995;2542-2547.
    • (1995) Cancer Res , vol.55 , pp. 2542-2547
    • Gasdaska, P.Y.1    Fisher, H.2    Powis, G.3
  • 53
    • 0028012886 scopus 로고
    • A two-domain structure for the two subunits of NAD(P)H:quinone acceptor oxidoreductase
    • Chen S., Deng P.S.-K., Bailey J., Swiderek K.M. A two-domain structure for the two subunits of NAD(P)H:quinone acceptor oxidoreductase. Protein Sci. 3:1994;51-57.
    • (1994) Protein Sci , vol.3 , pp. 51-57
    • Chen, S.1    Deng, P.S.-K.2    Bailey, J.3    Swiderek, K.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.