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Volumn 1113, Issue , 2014, Pages 167-186

Enzyme kinetics, inhibition, and regioselectivity of aldehyde oxidase

Author keywords

Aldehyde oxidase; Computational predictions; DACA; Drug metabolism; Drug drug interactions; Inhibition; Nitric oxide; Pharmacokinetics; Reactive oxygen species

Indexed keywords

6 (2 AMINO 4 PHENYLPYRIMIDIN 5 YL) 2 ISOPROPYLPYRIDAZIN 3(2H)ONE; 6 [6 (1 METHYL 1H PYRAZOL 4 YL) [1,2,4]TRIAZOLO[4,3 B]PYRIDAZIN 3 YLTHIO]QUINOLINE; ADENOSINE A1 RECEPTOR ANTAGONIST; ALDEHYDE OXIDASE; CYTOKINE RECEPTOR ANTAGONIST; FK 3453; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE P38 INHIBITOR; REACTIVE OXYGEN METABOLITE; SGX 523; SUPEROXIDE; UNCLASSIFIED DRUG;

EID: 84934443686     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-62703-758-7_9     Document Type: Article
Times cited : (17)

References (64)
  • 1
    • 79958841704 scopus 로고    scopus 로고
    • The kinetic mechanism for cytochrome P450 metabolism of Type II binding compounds: Evidence supporting direct reduction
    • doi:10. 1016/j.abb.2011.04.008
    • Pearson J, Dahal UP, Rock D, Peng C-C, Schenk JO, Joswig-Jones C, Jones JP (2011) The kinetic mechanism for cytochrome P450 metabolism of Type II binding compounds: Evidence supporting direct reduction. Arch Biochem Biophys 511(1-2):69-79. doi:10. 1016/j.abb.2011.04.008
    • (2011) Arch Biochem Biophys , vol.511 , Issue.1-2 , pp. 69-79
    • Pearson, J.1    Dahal, U.P.2    Rock, D.3    Peng, C.-C.4    Schenk, J.O.5    Joswig-Jones, C.6    Jones, J.P.7
  • 2
    • 84863408056 scopus 로고    scopus 로고
    • Comparative study of the affinity and metabolism of type i and type II binding quinoline carboxamide analogues by cytochrome P450 3A4
    • doi:10. 1021/jm201207h
    • Dahal UP, Joswig-Jones C, Jones JP (2012) Comparative study of the affinity and metabolism of type I and type II binding quinoline carboxamide analogues by cytochrome P450 3A4. J Med Chem 55(1):280-290. doi:10. 1021/jm201207h
    • (2012) J Med Chem , vol.55 , Issue.1 , pp. 280-290
    • Dahal, U.P.1    Joswig-Jones, C.2    Jones, J.P.3
  • 3
    • 78650379608 scopus 로고    scopus 로고
    • Aldehyde oxidase: An enzyme of emerging importance in drug discovery
    • doi:10.1021/jm100888d
    • Pryde DC, Dalvie D, Hu Q, Jones P, Obach RS, Tran T-D (2010) Aldehyde oxidase: An enzyme of emerging importance in drug discovery. J Med Chem 53(24):8441-8460. doi:10.1021/jm100888d
    • (2010) J Med Chem , vol.53 , Issue.24 , pp. 8441-8460
    • Pryde, D.C.1    Dalvie, D.2    Hu, Q.3    Jones, P.4    Obach, R.S.5    Tran, T.-D.6
  • 4
    • 0021831697 scopus 로고
    • Oxidative metabolism of carbazeran in vitro by liver cytosol of baboon and man
    • doi:10.3109/00498258509045354
    • Kaye B, Rance DJ, Waring L (1985) Oxidative metabolism of carbazeran in vitro by liver cytosol of baboon and man. Xenobiotica 15 (3):237-242. doi:10.3109/00498258509045354
    • (1985) Xenobiotica , vol.15 , Issue.3 , pp. 237-242
    • Kaye, B.1    Rance, D.J.2    Waring, L.3
  • 5
    • 84857383845 scopus 로고    scopus 로고
    • Deuterium isotope effects on drug pharmacokinetics. I. System-dependent effects of specific deuteration with aldehyde oxidase cleared drugs
    • doi:10. 1124/dmd.111.042770
    • Sharma R, Strelevitz TJ, Gao H, Clark AJ, Schildknegt K, Obach RS, Ripp SL, Spracklin DK, Tremaine LM, Vaz ADN (2012) Deuterium isotope effects on drug pharmacokinetics. I. System-dependent effects of specific deuteration with aldehyde oxidase cleared drugs. Drug Metab Dispos 40(3):625-634. doi:10. 1124/dmd.111.042770
    • (2012) Drug Metab Dispos , vol.40 , Issue.3 , pp. 625-634
    • Sharma, R.1    Strelevitz, T.J.2    Gao, H.3    Clark, A.J.4    Schildknegt, K.5    Obach, R.S.6    Ripp, S.L.7    Spracklin, D.K.8    Tremaine, L.M.9    Adn, V.10
  • 6
    • 0022344589 scopus 로고
    • Guinea pig liver aldehyde oxidase as a sulfoxide reductase: Its purification and characterization
    • Yoshihara S, Tatsumi K (1985) Guinea pig liver aldehyde oxidase as a sulfoxide reductase: Its purification and characterization. Arch Biochem Biophys 242(1):213-224
    • (1985) Arch Biochem Biophys , vol.242 , Issue.1 , pp. 213-224
    • Yoshihara, S.1    Tatsumi, K.2
  • 7
    • 0021279818 scopus 로고
    • Reduction of tertiary amine N-oxides by liver preparations: Function of aldehyde oxidase as a major Noxide reductase
    • Kitamura S, Tatsumi K (1984) Reduction of tertiary amine N-oxides by liver preparations: Function of aldehyde oxidase as a major Noxide reductase. Biochem Biophys Res Commun 121(3):749-754
    • (1984) Biochem Biophys Res Commun , vol.121 , Issue.3 , pp. 749-754
    • Kitamura, S.1    Tatsumi, K.2
  • 8
    • 0018606104 scopus 로고
    • The enzyme aldehyde oxidase is an iminium oxidase. Reaction with nicotine delta 10(50) iminium ion
    • Brandaenge S, Lindblom L (1979) The enzyme ?aldehyde oxidase? is an iminium oxidase. Reaction with nicotine delta 10(50) iminium ion. Biochem Biophys Res Commun 91:991-996
    • (1979) Biochem Biophys Res Commun , vol.91 , pp. 991-996
    • Brandaenge, S.1    Lindblom, L.2
  • 9
    • 79960719085 scopus 로고    scopus 로고
    • Increasing recognition of the importance of aldehyde oxidase in drug development and discovery
    • doi:10.3109/03602532. 2011.560606
    • Garattini E, Terao M (2011) Increasing recognition of the importance of aldehyde oxidase in drug development and discovery. Drug Metab Rev 43(3):374-386. doi:10.3109/03602532. 2011.560606
    • (2011) Drug Metab Rev , vol.43 , Issue.3 , pp. 374-386
    • Garattini, E.1    Terao, M.2
  • 10
    • 84858848617 scopus 로고    scopus 로고
    • The role of aldehyde oxidase in drug metabolism
    • doi:10. 1517/17425255.2012.663352
    • Garattini E, Terao M (2012) The role of aldehyde oxidase in drug metabolism. Expert Opin Drug Metab Toxicol 8(4):487-503. doi:10. 1517/17425255.2012.663352
    • (2012) Expert Opin Drug Metab Toxicol , vol.8 , Issue.4 , pp. 487-503
    • Garattini, E.1    Terao, M.2
  • 11
    • 34547690946 scopus 로고    scopus 로고
    • Biology of the molybdenum cofactor
    • Mendel RR (2007) Biology of the molybdenum cofactor. J Exp Bot 58(9):2289-2296
    • (2007) J Exp Bot , vol.58 , Issue.9 , pp. 2289-2296
    • Mendel, R.R.1
  • 13
    • 71049117283 scopus 로고    scopus 로고
    • Purification and mechanism of human aldehyde oxidase expressed in Escherichia coli
    • doi:10.1124/dmd.109.029520
    • Alfaro JF, Joswig-Jones CA, Ouyang W, Nichols J, Crouch GJ, Jones JP (2009) Purification and mechanism of human aldehyde oxidase expressed in Escherichia coli. Drug Metab Dispos 37(12):2393-2398. doi:10.1124/dmd.109.029520
    • (2009) Drug Metab Dispos , vol.37 , Issue.12 , pp. 2393-2398
    • Alfaro, J.F.1    Joswig-Jones, C.A.2    Ouyang, W.3    Nichols, J.4    Crouch, G.J.5    Jones, J.P.6
  • 16
    • 33744979094 scopus 로고    scopus 로고
    • Drugmetabolizing ability of molybdenum hydroxylases
    • Kitamura S, Sugihara K, Ohta S (2006) Drugmetabolizing ability of molybdenum hydroxylases. Drug Metab Pharmacokinet 21 (2):83-98
    • (2006) Drug Metab Pharmacokinet , vol.21 , Issue.2 , pp. 83-98
    • Kitamura, S.1    Sugihara, K.2    Ohta, S.3
  • 17
    • 0029155308 scopus 로고
    • Acidic metabolites of tamoxifen. Aspects of formation and fate in the female rat
    • Ruenitz PC, Bai X (1995) Acidic metabolites of tamoxifen. Aspects of formation and fate in the female rat. Drug Metab Dispos 23(9): 993-998
    • (1995) Drug Metab Dispos , vol.23 , Issue.9 , pp. 993-998
    • Ruenitz, P.C.1    Bai, X.2
  • 19
    • 13844294285 scopus 로고    scopus 로고
    • Identification of aldehyde oxidase as the neonicotinoid nitroreductase
    • doi:10.1021/tx049737i
    • Dick RA, Kanne DB, Casida JE (2005) Identification of aldehyde oxidase as the neonicotinoid nitroreductase. Chem Res Toxicol 18 (2):317-323. doi:10.1021/tx049737i
    • (2005) Chem Res Toxicol , vol.18 , Issue.2 , pp. 317-323
    • Dick, R.A.1    Kanne, D.B.2    Casida, J.E.3
  • 20
    • 31844451913 scopus 로고    scopus 로고
    • Substrate specificity of rabbit aldehyde oxidase for nitroguanidine and nitromethylene neonicotinoid insecticides
    • doi:10.1021/tx050230x
    • Dick RA, Kanne DB, Casida JE (2006) Substrate specificity of rabbit aldehyde oxidase for nitroguanidine and nitromethylene neonicotinoid insecticides. Chem Res Toxicol 19 (1):38-43. doi:10.1021/tx050230x
    • (2006) Chem Res Toxicol , vol.19 , Issue.1 , pp. 38-43
    • Dick, R.A.1    Kanne, D.B.2    Casida, J.E.3
  • 21
    • 0030058077 scopus 로고    scopus 로고
    • Involvement of mammalian liver cytosols and aldehyde oxidase in reductive metabolism of zonisamide
    • Sugihara K, Kitamura S, Tatsumi K (1996) Involvement of mammalian liver cytosols and aldehyde oxidase in reductive metabolism of zonisamide. Drug Metab Dispos 24 (2):199-202
    • (1996) Drug Metab Dispos , vol.24 , Issue.2 , pp. 199-202
    • Sugihara, K.1    Kitamura, S.2    Tatsumi, K.3
  • 22
    • 0032962715 scopus 로고    scopus 로고
    • Aldehyde oxidase-dependent marked species difference in hepatic metabolism of the sedative-hypnotic, zaleplon, between monkeys and rats
    • Kawashima K, Hosoi K, Naruke T, Shiba T, Kitamura M, Watabe T (1999) Aldehyde oxidase-dependent marked species difference in hepatic metabolism of the sedative-hypnotic, zaleplon, between monkeys and rats. Drug Metab Dispos 27(3):422-428
    • (1999) Drug Metab Dispos , vol.27 , Issue.3 , pp. 422-428
    • Kawashima, K.1    Hosoi, K.2    Naruke, T.3    Shiba, T.4    Kitamura, M.5    Watabe, T.6
  • 23
    • 0036795513 scopus 로고    scopus 로고
    • Metabolism of zaleplon by human liver: Evidence for involvement of aldehyde oxidase
    • doi:10.1080/00498250210158915
    • Lake BG, Ball SE, Kao J, Renwick AB, Price RJ, Scatina JA (2002) Metabolism of zaleplon by human liver: Evidence for involvement of aldehyde oxidase. Xenobiotica 32(10):835-847. doi:10.1080/00498250210158915
    • (2002) Xenobiotica , vol.32 , Issue.10 , pp. 835-847
    • Lake, B.G.1    Ball, S.E.2    Kao, J.3    Renwick, A.B.4    Price, R.J.5    Scatina, J.A.6
  • 24
    • 0034071009 scopus 로고    scopus 로고
    • Species differences in oral bioavailability of methotrexate between rats and monkeys
    • Kuroda T, Namba K, Torimaru T, Kawashima K, HayashiM(2000) Species differences in oral bioavailability of methotrexate between rats and monkeys. Biol Pharm Bull 23(3):334-338
    • (2000) Biol Pharm Bull , vol.23 , Issue.3 , pp. 334-338
    • Kuroda, T.1    Namba, K.2    Torimaru, T.3    Kawashima, K.4    Hayashi, M.5
  • 25
    • 27744561770 scopus 로고    scopus 로고
    • Zebularine metabolism by aldehyde oxidase in hepatic cytosol from humans, monkeys, dogs, rats, and mice: Influence of sex and inhibitors
    • doi:10. 1016/j.bmc.2005.07.053
    • Klecker RW, Cysyk RL, Collins JM (2006) Zebularine metabolism by aldehyde oxidase in hepatic cytosol from humans, monkeys, dogs, rats, and mice: Influence of sex and inhibitors. Bioorg Med Chem 14(1):62-66. doi:10. 1016/j.bmc.2005.07.053
    • (2006) Bioorg Med Chem , vol.14 , Issue.1 , pp. 62-66
    • Klecker, R.W.1    Cysyk, R.L.2    Collins, J.M.3
  • 26
    • 34848819742 scopus 로고    scopus 로고
    • In vitro study of 6-mercaptopurine oxidation catalysed by aldehyde oxidase and xanthine oxidase
    • Rashidi M-R, Beedham C, Smith JS, Davaran S (2007) In vitro study of 6-mercaptopurine oxidation catalysed by aldehyde oxidase and xanthine oxidase. Drug Metab Pharmacokinet 22 (4):299-306
    • (2007) Drug Metab Pharmacokinet , vol.22 , Issue.4 , pp. 299-306
    • Rashidi, M.-R.1    Beedham, C.2    Smith, J.S.3    Davaran, S.4
  • 27
    • 79954525297 scopus 로고    scopus 로고
    • Case report of extensive metabolism by aldehyde oxidase in humans: Pharmacokinetics and metabolite profile of FK3453 in rats, dogs, and humans
    • doi:10.3109/00498254. 2010.549970
    • Akabane T, Tanaka K, Irie M, Terashita S, Teramura T (2011) Case report of extensive metabolism by aldehyde oxidase in humans: Pharmacokinetics and metabolite profile of FK3453 in rats, dogs, and humans. Xenobiotica 41(5):372-384. doi:10.3109/00498254. 2010.549970
    • (2011) Xenobiotica , vol.41 , Issue.5 , pp. 372-384
    • Akabane, T.1    Tanaka, K.2    Irie, M.3    Terashita, S.4    Teramura, T.5
  • 28
    • 84455171514 scopus 로고    scopus 로고
    • Prediction of human metabolism of FK3453 by aldehyde oxidase using chimeric mice transplanted with human or rat hepatocytes
    • doi:10.1124/dmd.111.041954
    • Sanoh S, Nozaki K, Murai H, Terashita S, Teramura T, Ohta S (2012) Prediction of human metabolism of FK3453 by aldehyde oxidase using chimeric mice transplanted with human or rat hepatocytes. Drug Metab Dispos 40 (1):76-82. doi:10.1124/dmd.111.041954
    • (2012) Drug Metab Dispos , vol.40 , Issue.1 , pp. 76-82
    • Sanoh, S.1    Nozaki, K.2    Murai, H.3    Terashita, S.4    Teramura, T.5    Ohta, S.6
  • 29
    • 77954936842 scopus 로고    scopus 로고
    • Speciesspecific metabolism of SGX523 by aldehyde oxidase and the toxicological implications
    • doi:10. 1124/dmd.110.032375
    • Diamond S, Boer J, Maduskuie T, Falahatpisheh N, Li Y, Yeleswaram S (2010) Speciesspecific metabolism of SGX523 by aldehyde oxidase and the toxicological implications. Drug Metab Dispos 38:1277-1285. doi:10. 1124/dmd.110.032375
    • (2010) Drug Metab Dispos , vol.38 , pp. 1277-1285
    • Diamond, S.1    Boer, J.2    Maduskuie, T.3    Falahatpisheh, N.4    Li, Y.5    Yeleswaram, S.6
  • 30
    • 78650303504 scopus 로고    scopus 로고
    • In silico and in vitro pharmacogenetics: Aldehyde oxidase rapidly metabolizes a p38 kinase inhibitor
    • doi:10.1038/tpj.2010.8
    • Zhang X, Liu H-H,Weller P, Zheng M, TaoW, Wang J, Liao G, Monshouwer M, Peltz G (2010) In silico and in vitro pharmacogenetics: Aldehyde oxidase rapidly metabolizes a p38 kinase inhibitor. Pharmacogenomics J 11:15-24. doi:10.1038/tpj.2010.8
    • (2010) Pharmacogenomics J , vol.11 , pp. 15-24
    • Zhang, X.1    Liu, H.-H.2    Weller, P.3    Zheng, M.4    Tao, W.5    Wang, J.6    Liao, G.7    Monshouwer, M.8    Peltz, G.9
  • 31
    • 71749090061 scopus 로고    scopus 로고
    • Characterization of the magnitude and mechanism of aldehyde oxidase-mediated nitric oxide production from nitrite
    • doi:10.1074/jbc.M109. 019125
    • Li H, Kundu TK, Zweier JL (2009) Characterization of the magnitude and mechanism of aldehyde oxidase-mediated nitric oxide production from nitrite. J Biol Chem 284 (49):33850-33858. doi:10.1074/jbc.M109. 019125
    • (2009) J Biol Chem , vol.284 , Issue.49 , pp. 33850-33858
    • Li, H.1    Kundu, T.K.2    Zweier, J.L.3
  • 32
    • 49649118849 scopus 로고    scopus 로고
    • Nitric oxide production from nitrite occurs primarily in tissues not in the blood: Critical role of xanthine oxidase and aldehyde oxidase
    • doi:10.1074/jbc.M801785200
    • Li H, Cui H, Kundu TK, Alzawahra W, Zweier JL (2008) Nitric oxide production from nitrite occurs primarily in tissues not in the blood: Critical role of xanthine oxidase and aldehyde oxidase. J Biol Chem 283(26):17855-17863. doi:10.1074/jbc.M801785200
    • (2008) J Biol Chem , vol.283 , Issue.26 , pp. 17855-17863
    • Li, H.1    Cui, H.2    Kundu, T.K.3    Alzawahra, W.4    Zweier, J.L.5
  • 33
    • 0029680493 scopus 로고    scopus 로고
    • Carbon dioxide: Physiological catalyst for peroxynitritemediated cellular damage or cellular protectant
    • doi:10.1021/tx960046z
    • Lymar SV, Hurst JK (1996) Carbon dioxide: Physiological catalyst for peroxynitritemediated cellular damage or cellular protectant Chem Res Toxicol 9(5):845-850. doi:10.1021/tx960046z
    • (1996) Chem Res Toxicol , vol.9 , Issue.5 , pp. 845-850
    • Lymar, S.V.1    Hurst, J.K.2
  • 34
    • 0028991318 scopus 로고
    • The reaction of NO. with O2.-and HO2. A pulse radiolysis study
    • Goldstein S, Czapski G (1995) The reaction of NO. with O2.-and HO2.: A pulse radiolysis study. Free Radic Biol Med 19(4):505-510
    • (1995) Free Radic Biol Med , vol.19 , Issue.4 , pp. 505-510
    • Goldstein, S.1    Czapski, G.2
  • 35
    • 0028970801 scopus 로고
    • The role of the reactions of .NO with superoxide and oxygen in biological systems: A kinetic approach
    • Czapski G, Goldstein S (1995) The role of the reactions of .NO with superoxide and oxygen in biological systems: A kinetic approach. Free Radic Biol Med 19(6):785-794
    • (1995) Free Radic Biol Med , vol.19 , Issue.6 , pp. 785-794
    • Czapski, G.1    Goldstein, S.2
  • 36
    • 84859385695 scopus 로고    scopus 로고
    • Aldehyde oxidase functions as a superoxide generating NADH oxidase: An important redox regulated pathway of cellular oxygen radical formation
    • doi:10.1021/bi3000879
    • Kundu TK, Velayutham M, Zweier JL (2012) Aldehyde oxidase functions as a superoxide generating NADH oxidase: An important redox regulated pathway of cellular oxygen radical formation. Biochemistry 51 (13):2930-2939. doi:10.1021/bi3000879
    • (2012) Biochemistry , vol.51 , Issue.13 , pp. 2930-2939
    • Kundu, T.K.1    Velayutham, M.2    Zweier, J.L.3
  • 37
    • 33947723940 scopus 로고    scopus 로고
    • Characterization of superoxide production from aldehyde oxidase: An important source of oxidants in biological tissues
    • doi:10. 1016/j.abb.2006.12.032
    • Kundu TK, Hille R, Velayutham M, Zweier JL (2007) Characterization of superoxide production from aldehyde oxidase: An important source of oxidants in biological tissues. Arch Biochem Biophys 460(1):113-121. doi:10. 1016/j.abb.2006.12.032
    • (2007) Arch Biochem Biophys , vol.460 , Issue.1 , pp. 113-121
    • Kundu, T.K.1    Hille, R.2    Velayutham, M.3    Zweier, J.L.4
  • 38
    • 0035824605 scopus 로고    scopus 로고
    • Purification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of a novel molybdo-flavoprotein gene cluster on mouse chromosome
    • doi:10.1074/jbc. M105744200
    • Terao M, Kurosaki M, Marini M, Vanoni MA, Saltini G, Bonetto V, Bastone A, Federico C, Saccone S, Fanelli R, Salmona M, Garattini E (2001) Purification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of a novel molybdo-flavoprotein gene cluster on mouse chromosome. J Biol Chem 276 (49):46347-46363. doi:10.1074/jbc. M105744200
    • (2001) J Biol Chem , vol.276 , Issue.49 , pp. 46347-46363
    • Terao, M.1    Kurosaki, M.2    Marini, M.3    Vanoni, M.A.4    Saltini, G.5    Bonetto, V.6    Bastone, A.7    Federico, C.8    Saccone, S.9    Fanelli, R.10    Salmona, M.11    Garattini, E.12
  • 39
    • 9644262449 scopus 로고    scopus 로고
    • The aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase homologue 3, a novel member of the molybdoflavoenzyme family with selective expression in the olfactory mucosa
    • doi:10.1074/jbc. M408734200
    • Kurosaki M, Terao M, Barzago MM, Bastone A, Bernardinello D, Salmona M, Garattini E (2004) The aldehyde oxidase gene cluster in mice and rats. Aldehyde oxidase homologue 3, a novel member of the molybdoflavoenzyme family with selective expression in the olfactory mucosa. J Biol Chem 279 (48):50482-50498. doi:10.1074/jbc. M408734200
    • (2004) J Biol Chem , vol.279 , Issue.48 , pp. 50482-50498
    • Kurosaki, M.1    Terao, M.2    Barzago, M.M.3    Bastone, A.4    Bernardinello, D.5    Salmona, M.6    Garattini, E.7
  • 40
    • 0032104270 scopus 로고    scopus 로고
    • Isolation and characterization of the human aldehyde oxidase gene: Conservation of intron/exon boundaries with the xanthine oxidoreductase gene indicates a common origin
    • Terao M, Kurosaki M, Demontis S, Zanotta S, Garattini E (1998) Isolation and characterization of the human aldehyde oxidase gene: Conservation of intron/exon boundaries with the xanthine oxidoreductase gene indicates a common origin. Biochem J 332(Pt 2):383-393
    • (1998) Biochem J , vol.332 , Issue.PART 2 , pp. 383-393
    • Terao, M.1    Kurosaki, M.2    Demontis, S.3    Zanotta, S.4    Garattini, E.5
  • 41
    • 0033166759 scopus 로고    scopus 로고
    • Molecular cloning of the cDNA coding for mouse aldehyde oxidase: Tissue distribution and regulation in vivo by testosterone
    • Kurosaki M, Demontis S, Barzago MM, Garattini E, Terao M (1999) Molecular cloning of the cDNA coding for mouse aldehyde oxidase: Tissue distribution and regulation in vivo by testosterone. Biochem J 341(Pt 1):71-80
    • (1999) Biochem J , vol.341 , Issue.PART 1 , pp. 71-80
    • Kurosaki, M.1    Demontis, S.2    Barzago, M.M.3    Garattini, E.4    Terao, M.5
  • 43
    • 0015084372 scopus 로고
    • Aldehyde oxidase: Catalysis of the oxidation of N 1-methylnicotinamide and pyridoxal
    • Stanulovic? M, Chaykin S (1971) Aldehyde oxidase: Catalysis of the oxidation of N 1-methylnicotinamide and pyridoxal. Arch Biochem Biophys 145(1):27-34
    • (1971) Arch Biochem Biophys , vol.145 , Issue.1 , pp. 27-34
    • Stanulovic, M.1    Chaykin, S.2
  • 44
    • 0033585012 scopus 로고    scopus 로고
    • Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney
    • Ambroziak W, Izaguirre G, Pietruszko R (1999) Metabolism of retinaldehyde and other aldehydes in soluble extracts of human liver and kidney. J Biol Chem 274 (47):33366-33373
    • (1999) J Biol Chem , vol.274 , Issue.47 , pp. 33366-33373
    • Ambroziak, W.1    Izaguirre, G.2    Pietruszko, R.3
  • 46
    • 0029025709 scopus 로고
    • Substrate specificity of human liver aldehyde oxidase toward substituted quinazolines and phthalazines: A comparison with hepatic enzyme from guinea pig, rabbit, and baboon
    • Beedham C, Critchley DJ, Rance DJ (1995) Substrate specificity of human liver aldehyde oxidase toward substituted quinazolines and phthalazines: A comparison with hepatic enzyme from guinea pig, rabbit, and baboon. Arch Biochem Biophys 319(2):481-490
    • (1995) Arch Biochem Biophys , vol.319 , Issue.2 , pp. 481-490
    • Beedham, C.1    Critchley, D.J.2    Rance, D.J.3
  • 47
    • 0347364803 scopus 로고    scopus 로고
    • Human liver aldehyde oxidase: Inhibition by 239 drugs
    • Obach RS, Huynh P, Allen MC, Beedham C (2004) Human liver aldehyde oxidase: Inhibition by 239 drugs. J Clin Pharmacol 44 (1):7-19
    • (2004) J Clin Pharmacol , vol.44 , Issue.1 , pp. 7-19
    • Obach, R.S.1    Huynh, P.2    Allen, M.C.3    Beedham, C.4
  • 48
    • 34648830277 scopus 로고    scopus 로고
    • Use of density functional calculations to predict the regioselectivity of drugs and molecules metabolized by aldehyde oxidase
    • Torres RA, Korzekwa KR, McMasters DR, Fandozzi CM, Jones JP (2007) Use of density functional calculations to predict the regioselectivity of drugs and molecules metabolized by aldehyde oxidase. J Med Chem 50 (19):4642-4647
    • (2007) J Med Chem , vol.50 , Issue.19 , pp. 4642-4647
    • Torres, R.A.1    Korzekwa, K.R.2    McMasters, D.R.3    Fandozzi, C.M.4    Jones, J.P.5
  • 49
    • 84871575600 scopus 로고    scopus 로고
    • Evidence for substrate dependent inhibition profiles for human liver aldehyde oxidase
    • doi:10. 1124/dmd.112.048546
    • Barr JT, Jones JP (2012) Evidence for substrate dependent inhibition profiles for human liver aldehyde oxidase. Drug Metab Dispos. doi:10. 1124/dmd.112.048546
    • (2012) Drug Metab Dispos
    • Barr, J.T.1    Jones, J.P.2
  • 50
    • 81855217400 scopus 로고    scopus 로고
    • Inhibition of human liver aldehyde oxidase: Implications for potential drug-drug interactions
    • doi:10.1124/dmd. 111.041806
    • Barr J, Jones J (2011) Inhibition of human liver aldehyde oxidase: Implications for potential drug-drug interactions. Drug Metab Dispos 39(12):2381-2386. doi:10.1124/dmd. 111.041806
    • (2011) Drug Metab Dispos , vol.39 , Issue.12 , pp. 2381-2386
    • Barr, J.1    Jones, J.2
  • 51
    • 84455163212 scopus 로고    scopus 로고
    • Prediction of CYP2D6 drug interactions from in vitro data: Evidence for substrate-dependent inhibition
    • doi:10.1124/dmd.111.041210
    • Vandenbrink BM, Foti RS, Rock DA,Wienkers LC, Wahlstrom JL (2011) Prediction of CYP2D6 drug interactions from in vitro data: Evidence for substrate-dependent inhibition. Drug Metab Dispos 40:47-53. doi:10.1124/dmd.111. 041210
    • (2011) Drug Metab Dispos , vol.40 , pp. 47-53
    • Vandenbrink, B.M.1    Foti, R.S.2    Rock, D.A.3    Wienkers, L.C.4    Wahlstrom, J.L.5
  • 52
    • 33750547308 scopus 로고    scopus 로고
    • CYP2C9 inhibition: Impact of probe selection and pharmacogenetics on in vitro inhibition profiles
    • Kumar V,Wahlstrom JL, Rock DA,Warren CJ, Gorman LA, Tracy TS (2006) CYP2C9 inhibition: Impact of probe selection and pharmacogenetics on in vitro inhibition profiles. Drug Metab Dispos 34(12):1966-1975
    • (2006) Drug Metab Dispos , vol.34 , Issue.12 , pp. 1966-1975
    • Kumar, V.1    Wahlstrom, J.L.2    Rock, D.A.3    Warren, C.J.4    Gorman, L.A.5    Tracy, T.S.6
  • 53
    • 0020478588 scopus 로고
    • Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases
    • Wahl RC, Rajagopalan KV (1982) Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases. J Biol Chem 257 (3):1354-1359
    • (1982) J Biol Chem , vol.257 , Issue.3 , pp. 1354-1359
    • Wahl, R.C.1    Rajagopalan, K.V.2
  • 54
    • 0018246504 scopus 로고
    • Oxidation of quinazoline and quinoxaline by xanthine oxidase and aldehyde oxidase
    • doi:10. 1002/jhet.5570150802
    • Mccormack JJ, Allen BA, Hodnett CN (1978) Oxidation of quinazoline and quinoxaline by xanthine oxidase and aldehyde oxidase. J Heterocycl Chem 15(8):1249-1254. doi:10. 1002/jhet.5570150802
    • (1978) J Heterocycl Chem , vol.15 , Issue.8 , pp. 1249-1254
    • McCormack, J.J.1    Allen, B.A.2    Hodnett, C.N.3
  • 55
    • 38149011614 scopus 로고    scopus 로고
    • Nitroso-imidacloprid irreversibly inhibits rabbit aldehyde oxidase
    • doi:10.1021/tx700265r
    • Dick RA, Kanne DB, Casida JE (2007) Nitroso-imidacloprid irreversibly inhibits rabbit aldehyde oxidase. Chem Res Toxicol 20 (12):1942-1946. doi:10.1021/tx700265r
    • (2007) Chem Res Toxicol , vol.20 , Issue.12 , pp. 1942-1946
    • Dick, R.A.1    Kanne, D.B.2    Casida, J.E.3
  • 56
    • 0022408282 scopus 로고
    • Hydralazine: A potent inhibitor of aldehyde oxidase activity in vitro and in vivo
    • Johnson C, Stubley-Beedham C, Stell JG (1985) Hydralazine: A potent inhibitor of aldehyde oxidase activity in vitro and in vivo. Biochem Pharmacol 34(24):4251-4256
    • (1985) Biochem Pharmacol , vol.34 , Issue.24 , pp. 4251-4256
    • Johnson, C.1    Stubley-Beedham, C.2    Stell, J.G.3
  • 57
    • 84862681795 scopus 로고    scopus 로고
    • Hydralazine as a selective probe inactivator of aldehyde oxidase in human hepatocytes: Estimation of the contribution of aldehyde oxidase to metabolic clearance
    • doi:10.1124/dmd.112. 045195
    • Strelevitz TJ, Orozco CC, Obach RS (2012) Hydralazine as a selective probe inactivator of aldehyde oxidase in human hepatocytes: Estimation of the contribution of aldehyde oxidase to metabolic clearance. Drug Metab Dispos 40 (7):1441-1448. doi:10.1124/dmd.112. 045195
    • (2012) Drug Metab Dispos , vol.40 , Issue.7 , pp. 1441-1448
    • Strelevitz, T.J.1    Orozco, C.C.2    Obach, R.S.3
  • 58
    • 36949002370 scopus 로고    scopus 로고
    • Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: Roles of active site residues in binding and activation of purine substrate
    • Yamaguchi Y, Matsumura T, Ichida K, Okamoto K, Nishino T (2007) Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: Roles of active site residues in binding and activation of purine substrate. J Biochem 141 (4):513-524
    • (2007) J Biochem , vol.141 , Issue.4 , pp. 513-524
    • Yamaguchi, Y.1    Matsumura, T.2    Ichida, K.3    Okamoto, K.4    Nishino, T.5
  • 59
    • 0028832926 scopus 로고
    • Role of aldehyde oxidase in the in vitro conversion of famciclovir to penciclovir in human liver
    • Clarke SE, Harrell AW, Chenery RJ (1995) Role of aldehyde oxidase in the in vitro conversion of famciclovir to penciclovir in human liver. Drug Metab Dispos 23(2):251-254
    • (1995) Drug Metab Dispos , vol.23 , Issue.2 , pp. 251-254
    • Clarke, S.E.1    Harrell, A.W.2    Chenery, R.J.3
  • 60
    • 84862909119 scopus 로고    scopus 로고
    • Characterization of aldehyde oxidase enzyme activity in cryopreserved human hepatocytes
    • doi:10.1124/dmd.111.042861
    • Hutzler JM, Yang Y-S, Albaugh D, Fullenwider CL, Schmenk J, Fisher MB (2012) Characterization of aldehyde oxidase enzyme activity in cryopreserved human hepatocytes. Drug Metab Dispos 40(2):267-275. doi:10.1124/dmd.111.042861
    • (2012) Drug Metab Dispos , vol.40 , Issue.2 , pp. 267-275
    • Hutzler, J.M.1    Yang, Y.-S.2    Albaugh, D.3    Fullenwider, C.L.4    Schmenk, J.5    Fisher, M.B.6
  • 61
    • 0027411643 scopus 로고
    • Predicting the cytochrome P450 mediated metabolism of xenobiotics
    • Korzekwa KR, Jones JP (1993) Predicting the cytochrome P450 mediated metabolism of xenobiotics. Pharmacogenetics 3:1-18
    • (1993) Pharmacogenetics , vol.3 , pp. 1-18
    • Korzekwa, K.R.1    Jones, J.P.2
  • 62
    • 84863954854 scopus 로고    scopus 로고
    • Effect of structural variation on aldehyde oxidase-catalyzed oxidation of zoniporide
    • doi:10.1124/dmd.112. 045823
    • Dalvie D, Sun H, Xiang C, Hu Q, Jiang Y, Kang P (2012) Effect of structural variation on aldehyde oxidase-catalyzed oxidation of zoniporide. Drug Metab Dispos 40 (8):1575-1587. doi:10.1124/dmd.112. 045823
    • (2012) Drug Metab Dispos , vol.40 , Issue.8 , pp. 1575-1587
    • Dalvie, D.1    Sun, H.2    Xiang, C.3    Hu, Q.4    Jiang, Y.5    Kang, P.6
  • 63
    • 77954897164 scopus 로고    scopus 로고
    • In vitro-in vivo correlation for intrinsic clearance for drugs metabolized by human aldehyde oxidase
    • doi:10.1124/dmd.110.033555
    • ZientekM, Jiang Y, Youdim K,Obach RS (2010) In vitro-in vivo correlation for intrinsic clearance for drugs metabolized by human aldehyde oxidase. Drug Metab Dispos 38(8):1322-1327. doi:10.1124/dmd.110.033555
    • (2010) Drug Metab Dispos , vol.38 , Issue.8 , pp. 1322-1327
    • Zientekm Jiang, Y.1    Youdim, K.2    Obach, R.S.3
  • 64
    • 0030840879 scopus 로고    scopus 로고
    • In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde oxidase from human, guinea pig, rabbit, and rat liver
    • Rashidi MR, Smith JA, Clarke SE, Beedham C (1997) In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde oxidase from human, guinea pig, rabbit, and rat liver. Drug Metab Dispos 25(7):805-813
    • (1997) Drug Metab Dispos , vol.25 , Issue.7 , pp. 805-813
    • Rashidi, M.R.1    Smith, J.A.2    Clarke, S.E.3    Beedham, C.4


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