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Volumn 8, Issue 9, 2013, Pages

Mechanism of Porcine Liver Xanthine Oxidoreductase Mediated N-Oxide Reduction of Cyadox as Revealed by Docking and Mutagenesis Studies

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ASPARAGINE; ASPARTIC ACID; CIADOX; COMPLEMENTARY DNA; GLYCINE; LYSINE; SERINE; XANTHINE OXIDASE;

EID: 84883628770     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0073912     Document Type: Article
Times cited : (15)

References (44)
  • 2
    • 84855943310 scopus 로고    scopus 로고
    • Protein conformational gating of enzymatic activity in xanthine oxidoreductase
    • Ishikita H, Eger BT, Okamoto K, Nishino T, Pai EF, (2012) Protein conformational gating of enzymatic activity in xanthine oxidoreductase. J Am Chem Soc 134: 999-1009.
    • (2012) J Am Chem Soc , vol.134 , pp. 999-1009
    • Ishikita, H.1    Eger, B.T.2    Okamoto, K.3    Nishino, T.4    Pai, E.F.5
  • 3
    • 0028354118 scopus 로고
    • Mechanisms of reperfusion injury
    • Zimmerman BJ, Granger DN, (1994) Mechanisms of reperfusion injury. Am J Med Sci 307: 284-292.
    • (1994) Am J Med Sci , vol.307 , pp. 284-292
    • Zimmerman, B.J.1    Granger, D.N.2
  • 4
    • 0022343014 scopus 로고
    • Molybdenum hydroxylases as drug-metabolizing enzymes
    • Beedham C, (1985) Molybdenum hydroxylases as drug-metabolizing enzymes. Drug Metab Rev 16: 119-156.
    • (1985) Drug Metab Rev , vol.16 , pp. 119-156
    • Beedham, C.1
  • 5
    • 67649790241 scopus 로고    scopus 로고
    • Substrate orientation and catalysis at the molybdenum site in xanthine oxidase: Crystal structures in complex with xanthine and lumazine
    • Pauff JM, Cao H, Hille R, (2009) Substrate orientation and catalysis at the molybdenum site in xanthine oxidase: Crystal structures in complex with xanthine and lumazine. J Biol Chem 284: 8760-8767.
    • (2009) J Biol Chem , vol.284 , pp. 8760-8767
    • Pauff, J.M.1    Cao, H.2    Hille, R.3
  • 6
    • 77956233305 scopus 로고    scopus 로고
    • Substrate orientation and catalytic specificity in the action of xanthine oxidase: the sequential hydroxylation of hypoxanthine to uric acid
    • Cao H, Pauff JM, Hille R, (2010) Substrate orientation and catalytic specificity in the action of xanthine oxidase: the sequential hydroxylation of hypoxanthine to uric acid. J Biol Chem 285: 28044-28053.
    • (2010) J Biol Chem , vol.285 , pp. 28044-28053
    • Cao, H.1    Pauff, J.M.2    Hille, R.3
  • 7
    • 41949116623 scopus 로고    scopus 로고
    • Substrate orientation in xanthine oxidase: crystal structure of enzyme in reaction with 2-hydroxy-6-methylpurine
    • Pauff JM, Zhang J, Bell CE, Hille R, (2008) Substrate orientation in xanthine oxidase: crystal structure of enzyme in reaction with 2-hydroxy-6-methylpurine. J Biol Chem 283: 4818-4824.
    • (2008) J Biol Chem , vol.283 , pp. 4818-4824
    • Pauff, J.M.1    Zhang, J.2    Bell, C.E.3    Hille, R.4
  • 8
    • 78650800027 scopus 로고    scopus 로고
    • FYX-051: a novel and potent hybrid-type inhibitor of xanthine oxidoreductase
    • Matsumoto K, Okamoto K, Ashizawa N, Nishino T, (2011) FYX-051: a novel and potent hybrid-type inhibitor of xanthine oxidoreductase. J Pharmacol Exp Ther 336: 95-103.
    • (2011) J Pharmacol Exp Ther , vol.336 , pp. 95-103
    • Matsumoto, K.1    Okamoto, K.2    Ashizawa, N.3    Nishino, T.4
  • 9
    • 44949262935 scopus 로고    scopus 로고
    • Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase
    • Nishino T, Okamoto K, Eger BT, Pai EF, Nishino T, (2008) Mammalian xanthine oxidoreductase- mechanism of transition from xanthine dehydrogenase to xanthine oxidase. Febs J 275: 3278-3289.
    • (2008) Febs J , vol.275 , pp. 3278-3289
    • Nishino, T.1    Okamoto, K.2    Eger, B.T.3    Pai, E.F.4    Nishino, T.5
  • 10
    • 0034718556 scopus 로고    scopus 로고
    • Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion
    • Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, et al. (2000) Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc Natl Acad Sci U S A 97: 10723-10728.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10723-10728
    • Enroth, C.1    Eger, B.T.2    Okamoto, K.3    Nishino, T.4    Nishino, T.5
  • 11
    • 23844472369 scopus 로고    scopus 로고
    • Quinoxaline 1,4-dioxide: a versatile scaffold endowed with manifold activities
    • Carta A, Corona P, Loriga M, (2005) Quinoxaline 1,4-dioxide: a versatile scaffold endowed with manifold activities. Curr Med Chem 12: 2259-2272.
    • (2005) Curr Med Chem , vol.12 , pp. 2259-2272
    • Carta, A.1    Corona, P.2    Loriga, M.3
  • 12
    • 28844458799 scopus 로고    scopus 로고
    • Subchronic oral toxicity study with cyadox in Wistar rats
    • Fang G, He Q, Zhou S, Wang D, Zhang Y, et al. (2006) Subchronic oral toxicity study with cyadox in Wistar rats. Food Chem Toxicol 44: 36-41.
    • (2006) Food Chem Toxicol , vol.44 , pp. 36-41
    • Fang, G.1    He, Q.2    Zhou, S.3    Wang, D.4    Zhang, Y.5
  • 15
    • 0025375354 scopus 로고
    • Clinical signs and performance of pigs treated with different doses of carbadox, cyadox and olaquindox
    • Nabuurs MJ, van der Molen EJ, de Graaf GJ, Jager LP, (1990) Clinical signs and performance of pigs treated with different doses of carbadox, cyadox and olaquindox. Zentralbl Veterinarmed A 37: 68-76.
    • (1990) Zentralbl Veterinarmed A , vol.37 , pp. 68-76
    • Nabuurs, M.J.1    van der Molen, E.J.2    de Graaf, G.J.3    Jager, L.P.4
  • 16
    • 2042535787 scopus 로고
    • Determination of cyadox and its metabolites in plasma by adsorptive voltammetry
    • Sestakova I, Kopanica M, (1988) Determination of cyadox and its metabolites in plasma by adsorptive voltammetry. Talanta 35: 816-818.
    • (1988) Talanta , vol.35 , pp. 816-818
    • Sestakova, I.1    Kopanica, M.2
  • 17
    • 67650360063 scopus 로고    scopus 로고
    • Metabolism of cyadox in rat, chicken and pig liver microsomes and identification of metabolites by accurate mass measurements using electrospray ionization hybrid ion trap/time-of-flight mass spectrometry
    • Liu Z, Huang L, Dai M, Chen D, Tao Y, et al. (2009) Metabolism of cyadox in rat, chicken and pig liver microsomes and identification of metabolites by accurate mass measurements using electrospray ionization hybrid ion trap/time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 23: 2026-2034.
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 2026-2034
    • Liu, Z.1    Huang, L.2    Dai, M.3    Chen, D.4    Tao, Y.5
  • 18
    • 80053296914 scopus 로고    scopus 로고
    • Metabolism of cyadox by the intestinal mucosa microsomes and gut flora of swine, and identification of metabolites by high-performance liquid chromatography combined with ion trap/time-of-flight mass spectrometry
    • Xu N, Huang L, Liu Z, Pan Y, Wang X, et al. (2011) Metabolism of cyadox by the intestinal mucosa microsomes and gut flora of swine, and identification of metabolites by high-performance liquid chromatography combined with ion trap/time-of-flight mass spectrometry. Rapid Commun Mass Spectrom 25: 2333-2344.
    • (2011) Rapid Commun Mass Spectrom , vol.25 , pp. 2333-2344
    • Xu, N.1    Huang, L.2    Liu, Z.3    Pan, Y.4    Wang, X.5
  • 19
    • 84862142558 scopus 로고    scopus 로고
    • In vitro metabolism of cyadox in rat, chicken and swine using ultra-performance liquid chromatography quadrupole time-of-flight mass spectrometry
    • Wu H, Li L, Shen J, Wang Y, Liu K, et al. (2012) In vitro metabolism of cyadox in rat, chicken and swine using ultra-performance liquid chromatography quadrupole time-of-flight mass spectrometry. J Pharm Biomed Anal 67-68: 175-185.
    • (2012) J Pharm Biomed Anal , vol.67-68 , pp. 175-185
    • Wu, H.1    Li, L.2    Shen, J.3    Wang, Y.4    Liu, K.5
  • 20
    • 80053947167 scopus 로고    scopus 로고
    • The mechanism of enzymatic and non-enzymatic N-oxide reductive metabolism of cyadox in pig liver
    • Zheng M, Jiang J, Wang J, Tang X, Ouyang M, et al. (2011) The mechanism of enzymatic and non-enzymatic N-oxide reductive metabolism of cyadox in pig liver. Xenobiotica 41: 964-971.
    • (2011) Xenobiotica , vol.41 , pp. 964-971
    • Zheng, M.1    Jiang, J.2    Wang, J.3    Tang, X.4    Ouyang, M.5
  • 21
    • 0034830902 scopus 로고    scopus 로고
    • Redox-activated, hypoxia-selective DNA cleavage by quinoxaline 1,4-di-N-oxide
    • Ganley B, Chowdhury G, Bhansali J, Daniels JS, Gates KS, (2001) Redox-activated, hypoxia-selective DNA cleavage by quinoxaline 1,4-di-N-oxide. Bioorg Med Chem 9: 2395-2401.
    • (2001) Bioorg Med Chem , vol.9 , pp. 2395-2401
    • Ganley, B.1    Chowdhury, G.2    Bhansali, J.3    Daniels, J.S.4    Gates, K.S.5
  • 22
    • 67349166987 scopus 로고    scopus 로고
    • Xenotransplantation of solid organs in the pig-to-primate model
    • Ekser B, Rigotti P, Gridelli B, Cooper DK, (2009) Xenotransplantation of solid organs in the pig-to-primate model. Transpl Immunol 21: 87-92.
    • (2009) Transpl Immunol , vol.21 , pp. 87-92
    • Ekser, B.1    Rigotti, P.2    Gridelli, B.3    Cooper, D.K.4
  • 23
    • 0029902763 scopus 로고    scopus 로고
    • Computational methods for biomolecular docking
    • Lengauer T, Rarey M, (1996) Computational methods for biomolecular docking. Curr Opin Struct Biol 6: 402-406.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 402-406
    • Lengauer, T.1    Rarey, M.2
  • 24
    • 76449121008 scopus 로고    scopus 로고
    • A comparative study of AutoDock and PMF scoring performances, and SAR of 2-substituted pyrazolotriazolopyrimidines and 4-substituted pyrazolopyrimidines as potent xanthine oxidase inhibitors
    • Ali HI, Fujita T, Akaho E, Nagamatsu T, (2010) A comparative study of AutoDock and PMF scoring performances, and SAR of 2-substituted pyrazolotriazolopyrimidines and 4-substituted pyrazolopyrimidines as potent xanthine oxidase inhibitors. J Comput Aided Mol Des 24: 57-75.
    • (2010) J Comput Aided Mol Des , vol.24 , pp. 57-75
    • Ali, H.I.1    Fujita, T.2    Akaho, E.3    Nagamatsu, T.4
  • 25
    • 0034029284 scopus 로고    scopus 로고
    • Sequence motif-specific assignment of two [2Fe-2S] clusters in rat xanthine oxidoreductase studied by site-directed mutagenesis
    • Iwasaki T, Okamoto K, Nishino T, Mizushima J, Hori H, (2000) Sequence motif-specific assignment of two [2Fe-2S] clusters in rat xanthine oxidoreductase studied by site-directed mutagenesis. J Biochem 127: 771-778.
    • (2000) J Biochem , vol.127 , pp. 771-778
    • Iwasaki, T.1    Okamoto, K.2    Nishino, T.3    Mizushima, J.4    Hori, H.5
  • 26
    • 38449123646 scopus 로고    scopus 로고
    • Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase
    • Asai R, Nishino T, Matsumura T, Okamoto K, Igarashi K, et al. (2007) Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase. J Biochem 141: 525-534.
    • (2007) J Biochem , vol.141 , pp. 525-534
    • Asai, R.1    Nishino, T.2    Matsumura, T.3    Okamoto, K.4    Igarashi, K.5
  • 27
    • 0025143109 scopus 로고
    • Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin
    • Amaya Y, Yamazaki K, Sato M, Noda K, Nishino T, et al. (1990) Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin. J Biol Chem 265: 14170-14175.
    • (1990) J Biol Chem , vol.265 , pp. 14170-14175
    • Amaya, Y.1    Yamazaki, K.2    Sato, M.3    Noda, K.4    Nishino, T.5
  • 28
    • 0026520774 scopus 로고
    • Molecular cloning of a cDNA coding for mouse liver xanthine dehydrogenase. Regulation of its transcript by interferons in vivo
    • Terao M, Cazzaniga G, Ghezzi P, Bianchi M, Falciani F, et al. (1992) Molecular cloning of a cDNA coding for mouse liver xanthine dehydrogenase. Regulation of its transcript by interferons in vivo. Biochem J 283 (Pt 3): 863-870.
    • (1992) Biochem J , vol.283 , Issue.PART 3 , pp. 863-870
    • Terao, M.1    Cazzaniga, G.2    Ghezzi, P.3    Bianchi, M.4    Falciani, F.5
  • 29
    • 0027438935 scopus 로고
    • Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene
    • Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, et al. (1993) Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene 133: 279-284.
    • (1993) Gene , vol.133 , pp. 279-284
    • Ichida, K.1    Amaya, Y.2    Noda, K.3    Minoshima, S.4    Hosoya, T.5
  • 30
    • 0030077060 scopus 로고    scopus 로고
    • Purification of the bovine xanthine oxidoreductase from milk fat globule membranes and cloning of complementary deoxyribonucleic acid
    • Berglund L, Rasmussen JT, Andersen MD, Rasmussen MS, Petersen TE, (1996) Purification of the bovine xanthine oxidoreductase from milk fat globule membranes and cloning of complementary deoxyribonucleic acid. J Dairy Sci 79: 198-204.
    • (1996) J Dairy Sci , vol.79 , pp. 198-204
    • Berglund, L.1    Rasmussen, J.T.2    Andersen, M.D.3    Rasmussen, M.S.4    Petersen, T.E.5
  • 31
    • 0035291508 scopus 로고    scopus 로고
    • Molecular cloning of a cDNA coding for feline liver xanthine dehydrogenase
    • Tsuchida S, Yamada R, Ikemoto S, Tagawa M, (2001) Molecular cloning of a cDNA coding for feline liver xanthine dehydrogenase. J Vet Med Sci 63: 353-355.
    • (2001) J Vet Med Sci , vol.63 , pp. 353-355
    • Tsuchida, S.1    Yamada, R.2    Ikemoto, S.3    Tagawa, M.4
  • 32
    • 1842855681 scopus 로고    scopus 로고
    • Purification and characterization of multiple forms of rat liver xanthine oxidoreductase expressed in baculovirus-insect cell system
    • Nishino T, Amaya Y, Kawamoto S, Kashima Y, Okamoto K, et al. (2002) Purification and characterization of multiple forms of rat liver xanthine oxidoreductase expressed in baculovirus-insect cell system. J Biochem 132: 597-606.
    • (2002) J Biochem , vol.132 , pp. 597-606
    • Nishino, T.1    Amaya, Y.2    Kawamoto, S.3    Kashima, Y.4    Okamoto, K.5
  • 33
    • 3843146246 scopus 로고    scopus 로고
    • An efficient one-step site-directed and site-saturation mutagenesis protocol
    • Zheng L, Baumann U, Reymond JL, (2004) An efficient one-step site-directed and site-saturation mutagenesis protocol. Nucleic Acids Res 32: e115.
    • (2004) Nucleic Acids Res , vol.32
    • Zheng, L.1    Baumann, U.2    Reymond, J.L.3
  • 34
    • 0015243885 scopus 로고
    • Polypeptides of the tail fibres of bacteriophage T4
    • King J, Laemmli UK, (1971) Polypeptides of the tail fibres of bacteriophage T4. J Mol Biol 62: 465-477.
    • (1971) J Mol Biol , vol.62 , pp. 465-477
    • King, J.1    Laemmli, U.K.2
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
  • 37
    • 77958482893 scopus 로고    scopus 로고
    • Homology modeling, binding site identification and docking in flavone hydroxylase CYP105P2 in Streptomyces peucetius ATCC 27952
    • Kanth BK, Liou K, Sohng JK, (2010) Homology modeling, binding site identification and docking in flavone hydroxylase CYP105P2 in Streptomyces peucetius ATCC 27952. Comput Biol Chem 34: 226-231.
    • (2010) Comput Biol Chem , vol.34 , pp. 226-231
    • Kanth, B.K.1    Liou, K.2    Sohng, J.K.3
  • 38
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR
    • Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM, (1996) AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR 8: 477-486.
    • (1996) J Biomol NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 39
    • 0037449776 scopus 로고    scopus 로고
    • An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition
    • Okamoto K, Eger BT, Nishino T, Kondo S, Pai EF, et al. (2003) An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition. J Biol Chem 278: 1848-1855.
    • (2003) J Biol Chem , vol.278 , pp. 1848-1855
    • Okamoto, K.1    Eger, B.T.2    Nishino, T.3    Kondo, S.4    Pai, E.F.5
  • 40
    • 0034677969 scopus 로고    scopus 로고
    • Reduction of nitrite to nitric oxide catalyzed by xanthine oxidoreductase
    • Godber BL, Doel JJ, Sapkota GP, Blake DR, Stevens CR, et al. (2000) Reduction of nitrite to nitric oxide catalyzed by xanthine oxidoreductase. J Biol Chem 275: 7757-7763.
    • (2000) J Biol Chem , vol.275 , pp. 7757-7763
    • Godber, B.L.1    Doel, J.J.2    Sapkota, G.P.3    Blake, D.R.4    Stevens, C.R.5
  • 41
    • 0014028028 scopus 로고
    • Catalysis of the direct transfer of oxygen from nicotinamide N-oxide to xanthine by xanthine oxidase
    • Murray KN, Watson JG, Chaykin S, (1966) Catalysis of the direct transfer of oxygen from nicotinamide N-oxide to xanthine by xanthine oxidase. J Biol Chem 241: 4798-4801.
    • (1966) J Biol Chem , vol.241 , pp. 4798-4801
    • Murray, K.N.1    Watson, J.G.2    Chaykin, S.3
  • 42
    • 0027209264 scopus 로고
    • Redox potentials of milk xanthine dehydrogenase. Room temperature measurement of the FAD and 2Fe/2S center potentials
    • Hunt J, Massey V, Dunham WR, Sands RH, (1993) Redox potentials of milk xanthine dehydrogenase. Room temperature measurement of the FAD and 2Fe/2S center potentials. J Biol Chem 268: 18685-18691.
    • (1993) J Biol Chem , vol.268 , pp. 18685-18691
    • Hunt, J.1    Massey, V.2    Dunham, W.R.3    Sands, R.H.4
  • 43
    • 0020493623 scopus 로고
    • Oxidation-reduction potentials of molybdenum, flavin, and iron-sulfur centers in milk xanthine oxidase: variation with pH
    • Barber MJ, Siegel LM, (1982) Oxidation-reduction potentials of molybdenum, flavin, and iron-sulfur centers in milk xanthine oxidase: variation with pH. Biochemistry 21: 1638-1647.
    • (1982) Biochemistry , vol.21 , pp. 1638-1647
    • Barber, M.J.1    Siegel, L.M.2
  • 44
    • 0033742183 scopus 로고    scopus 로고
    • The role of the [2Fe-2s] cluster centers in xanthine oxidoreductase
    • Nishino T, Okamoto K, (2000) The role of the [2Fe-2s] cluster centers in xanthine oxidoreductase. J Inorg Biochem 82: 43-49.
    • (2000) J Inorg Biochem , vol.82 , pp. 43-49
    • Nishino, T.1    Okamoto, K.2


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