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Volumn 13, Issue 3, 2005, Pages 82-93

Molecular modelling of human aldehyde oxidase and identification of the key interactions in the enzyme-substrate complex

Author keywords

3D QSAR; Aldehyde oxidase; Genetic algorithm; Molecular modeling

Indexed keywords

ALDEHYDE OXIDASE; QUINAZOLINE DERIVATIVE; XANTHINE DEHYDROGENASE;

EID: 31644441318     PISSN: 15608115     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (22)

References (59)
  • 1
    • 31644441826 scopus 로고    scopus 로고
    • Drug metabolism
    • Williams DA, Lemke TL, editors. Philadelphia: Lippincott Williams and Wilkins
    • Williams DA. Drug metabolism. In: Williams DA, Lemke TL, editors. Foye's principles of medicinal chemistry. 5 ed. Philadelphia: Lippincott Williams and Wilkins; 2002. p 199-200.
    • (2002) Foye's Principles of Medicinal Chemistry. 5 Ed. , pp. 199-200
    • Williams, D.A.1
  • 2
    • 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. 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 1998; 332: 383-93.
    • (1998) Biochem J , vol.332 , pp. 383-393
    • Terao, M.1    Kurosaki, M.2    Demontis, S.3    Zanotta, S.4    Garattini, E.5
  • 3
    • 0023037533 scopus 로고
    • Aldehyde oxidase from rabbit liver: Specificity toward purines and their analogs
    • Hall WW, Krenitsky, T.A. Aldehyde oxidase from rabbit liver: Specificity toward purines and their analogs. Arch Biochem Biophys 1986; 251: 36-46.
    • (1986) Arch Biochem Biophys , vol.251 , pp. 36-46
    • Hall, W.W.1    Krenitsky, T.A.2
  • 5
    • 0034843414 scopus 로고    scopus 로고
    • Quantitative study of the structural requirments of phtalazine/ quinazoline derivatives for interaction with human liver aldehyde oxidase
    • Ghafourian T, Rashidi MR. Quantitative study of the structural requirments of phtalazine/quinazoline derivatives for interaction with human liver aldehyde oxidase. Chem Pharm Bull 2001; 49: 1066-71.
    • (2001) Chem Pharm Bull , vol.49 , pp. 1066-1071
    • Ghafourian, T.1    Rashidi, M.R.2
  • 6
    • 0023528062 scopus 로고
    • Molybdenum hydroxylases: Biological distribution and substrate-inhibitor specifity
    • Ellis GP, West GB, editors. Amsterdam: Elseveir
    • Beedham C. Molybdenum hydroxylases: Biological distribution and substrate-inhibitor specifity. In: Ellis GP, West GB, editors. Prog Med Chem. Volume 24. Amsterdam: Elseveir; 1987. p 85-127.
    • (1987) Prog Med Chem , vol.24 , pp. 85-127
    • Beedham, C.1
  • 7
    • 0029025709 scopus 로고
    • Substrate specifity of human aldehyde oxidase towards substituted quinazolines and phthalazines: A comparison with hepatic enzyme from guinea pig, rabbit and baboon
    • Beedham C, Critchley DJP, Rance DJ. Substrate specifity of human aldehyde oxidase towards substituted quinazolines and phthalazines: A comparison with hepatic enzyme from guinea pig, rabbit and baboon. Arch Biochem Biophys 1995; 319: 481-90.
    • (1995) Arch Biochem Biophys , vol.319 , pp. 481-490
    • Beedham, C.1    Critchley, D.J.P.2    Rance, D.J.3
  • 9
    • 0036629252 scopus 로고    scopus 로고
    • Molybdenum and tungsten in biology
    • Hille R. Molybdenum and tungsten in biology. Trends Biochem Sci 2002; 27: 360-67.
    • (2002) Trends Biochem Sci , vol.27 , pp. 360-367
    • Hille, R.1
  • 10
    • 0033585012 scopus 로고    scopus 로고
    • Metabolism of retinaldehyde and other aldehydes in soluble extracts of human
    • Ambroziak W, Izaguirre, G., Pietruszko, R. Metabolism of retinaldehyde and other aldehydes in soluble extracts of human. J Biol Chem 1999; 274: 33366-73.
    • (1999) J Biol Chem , vol.274 , pp. 33366-33373
    • Ambroziak, W.1    Izaguirre, G.2    Pietruszko, R.3
  • 11
    • 0028832926 scopus 로고
    • Role of aldehyde oxidase in the in vitro conversion of famciclovir to penciclovir in human liver
    • Clarke SE, Harrell, A.W., Chenery, R.J. Role of aldehyde oxidase in the in vitro conversion of famciclovir to penciclovir in human liver. Drug Metab Dispos 1995; 23: 251-54.
    • (1995) Drug Metab Dispos , vol.23 , pp. 251-254
    • Clarke, S.E.1    Harrell, A.W.2    Chenery, R.J.3
  • 13
    • 0029898079 scopus 로고    scopus 로고
    • Clinical pharmacokinetics of low-dose pulse methotrexate in rheumatoid arthritis
    • Bannwarth B, Pehourcq F, Schaeverbeke T, Dehais J. Clinical pharmacokinetics of low-dose pulse methotrexate in rheumatoid arthritis. Clin Pharmacokinet 1996; 30: 194-210.
    • (1996) Clin Pharmacokinet , vol.30 , pp. 194-210
    • Bannwarth, B.1    Pehourcq, F.2    Schaeverbeke, T.3    Dehais, J.4
  • 17
    • 0036794380 scopus 로고    scopus 로고
    • Inhibition of zaleplon metabolism by cimetidine in the human liver: In vitro studies with subcellular fractions and precision-cut liver
    • Renwick AB, Ball SE, Tredger JM, Price RJ, Walters DG, Kao J, Scatina JA, Lake BG. Inhibition of zaleplon metabolism by cimetidine in the human liver: in vitro studies with subcellular fractions and precision-cut liver. Xenobiotica 2002; 32: 849-62.
    • (2002) Xenobiotica , vol.32 , pp. 849-862
    • Renwick, A.B.1    Ball, S.E.2    Tredger, J.M.3    Price, R.J.4    Walters, D.G.5    Kao, J.6    Scatina, J.A.7    Lake, B.G.8
  • 20
    • 0029415355 scopus 로고
    • Pharmacokinetics of O6-benzylguanine in rats and its metabolism by rat liver microsomes
    • Roy SK, Gupta E, Dolan ME. Pharmacokinetics of O6-benzylguanine in rats and its metabolism by rat liver microsomes. Drug Metab Dispos 1995; 23: 1394-99.
    • (1995) Drug Metab Dispos , vol.23 , pp. 1394-1399
    • Roy, S.K.1    Gupta, E.2    Dolan, M.E.3
  • 21
    • 0032435753 scopus 로고    scopus 로고
    • Involvement of hepatic aldehyde oxidase in conversion of 1-methyl-4-phenyl-2,3-dihydropyridinium (MPTP+) to 1-methyl-4-phenyl-5,6- dihydro-2-pyridone
    • Yoshihara S, Ohta S. Involvement of hepatic aldehyde oxidase in conversion of 1-methyl-4-phenyl-2,3-dihydropyridinium (MPTP+) to 1-methyl-4-phenyl-5,6-dihydro-2-pyridone. Arch Biochem Biophys 1998; 360: 93-98.
    • (1998) Arch Biochem Biophys , vol.360 , pp. 93-98
    • Yoshihara, S.1    Ohta, S.2
  • 23
    • 0028230803 scopus 로고
    • Use of rat and human in vitro systems to assess the effectiveness and enzymology of deoxyguanine analogs as prodrugs of an antiviral agent
    • Harrell AW, Wheeler SM, East P, Clarke SE, Chenery RJ. Use of rat and human in vitro systems to assess the effectiveness and enzymology of deoxyguanine analogs as prodrugs of an antiviral agent. Drug Metab Dispos 1994; 22: 189-93.
    • (1994) Drug Metab Dispos , vol.22 , pp. 189-193
    • Harrell, A.W.1    Wheeler, S.M.2    East, P.3    Clarke, S.E.4    Chenery, R.J.5
  • 25
    • 0026702860 scopus 로고
    • Metabolism of nicotine by human liver microsomes: Stereoselective formation of trans-nicotine N′-oxide
    • Cashman JR, Park SB, Yang ZC, Wrighton SA, 3rd. Jp, Benowitz NL. Metabolism of nicotine by human liver microsomes: stereoselective formation of trans-nicotine N′-oxide. Chem Res Toxicol 1992; 5: 639-46.
    • (1992) Chem Res Toxicol , vol.5 , pp. 639-646
    • Cashman, J.R.1    Park, S.B.2    Yang, Z.C.3    Wrighton III, S.A.Jp.4    Benowitz, N.L.5
  • 26
    • 0038722339 scopus 로고    scopus 로고
    • Ziprasidone metabolism, aldehyde oxidase, and clinical implications
    • Beedham C, Miceli JJ, Obach RS. Ziprasidone metabolism, aldehyde oxidase, and clinical implications. J Psychopharmacol 2003; 23: 229-32.
    • (2003) J Psychopharmacol , vol.23 , pp. 229-232
    • Beedham, C.1    Miceli, J.J.2    Obach, R.S.3
  • 27
    • 0036093932 scopus 로고    scopus 로고
    • Ziprasidone: The fifth atypical antipsychotic
    • Caley CF, Cooper CK. Ziprasidone: the fifth atypical antipsychotic. Ann Pharmacother 2002; 36: 839-51.
    • (2002) Ann Pharmacother , vol.36 , pp. 839-851
    • Caley, C.F.1    Cooper, C.K.2
  • 28
    • 1642539111 scopus 로고    scopus 로고
    • Potent inhibition of human liver aldehyde oxidase by raloxifene
    • Obach RS. Potent inhibition of human liver aldehyde oxidase by raloxifene. Drug Metab Dispos 2004; 32: 89-97.
    • (2004) Drug Metab Dispos , vol.32 , pp. 89-97
    • Obach, R.S.1
  • 29
    • 0028256155 scopus 로고
    • Methadone: A potent inhibitor of rat liver aldehyde oxidase
    • Robertson IG, Gamage RS. Methadone: a potent inhibitor of rat liver aldehyde oxidase. Biochem Pharmacol 1994; 47: 584-87.
    • (1994) Biochem Pharmacol , vol.47 , pp. 584-587
    • Robertson, I.G.1    Gamage, R.S.2
  • 30
    • 0027198768 scopus 로고
    • Inhibition by SKF-525A of the aldehyde oxidase-mediated metabolism of the experimental antitumor agent acridine carboxamide
    • Robertson IG, Bland TG. Inhibition by SKF-525A of the aldehyde oxidase-mediated metabolism of the experimental antitumor agent acridine carboxamide. Biochem Pharmacol 1993; 45: 2159-62.
    • (1993) Biochem Pharmacol , vol.45 , pp. 2159-2162
    • Robertson, I.G.1    Bland, T.G.2
  • 31
    • 0022408282 scopus 로고
    • Hydralazine: A potent inhibitor of aldehyde oxidase activity in vitro and in vivo
    • Johnson C, Stubley-Beedham C, Stell JG. Hydralazine: a potent inhibitor of aldehyde oxidase activity in vitro and in vivo. Biochem Pharmacol 1985; 34: 4251-56.
    • (1985) Biochem Pharmacol , vol.34 , pp. 4251-4256
    • Johnson, C.1    Stubley-Beedham, C.2    Stell, J.G.3
  • 32
    • 0019441864 scopus 로고
    • Effects of sex hormones on hepatic aldehyde oxidase activity C57BL/6J mice
    • S.M. V, Dachtler SL. Effects of sex hormones on hepatic aldehyde oxidase activity C57BL/6J mice. Horm Res 1981; 14: 250-59.
    • (1981) Horm Res , vol.14 , pp. 250-259
    • Dachtler, S.L.1
  • 33
    • 0017069418 scopus 로고
    • Importance of pharmacokinetic studies on cyclophosphamide (NSC-26271) in understanding its cytotoxic effect
    • Donelli MG, Bartosek I, A. G, Martini A, Colombo T, Pacciarini MA, Modica R. Importance of pharmacokinetic studies on cyclophosphamide (NSC-26271) in understanding its cytotoxic effect. Cancer Treat Res 1976; 60: 395-401.
    • (1976) Cancer Treat Res , vol.60 , pp. 395-401
    • Donelli, M.G.1    Bartosek, I.2    Martini, A.3    Colombo, T.4    Pacciarini, M.A.5    Modica, R.6
  • 37
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994; 22: 4673-80.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 38
    • 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, Pai EF. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion. Biochemistry 2000; 97: 10723-28.
    • (2000) Biochemistry , vol.97 , pp. 10723-10728
    • Enroth, C.1    Eger, B.T.2    Okamoto, K.3    Nishino, T.4    Pai, E.F.5
  • 39
    • 0028865588 scopus 로고
    • Successful protein fold recognition by optimal sequence threading validated by rigorous blind testing
    • Jones DT, Miller RT, Thornton JM. Successful protein fold recognition by optimal sequence threading validated by rigorous blind testing. Proteins: Struct, Funct, Genet 1995; 23: 387-97.
    • (1995) Proteins: Struct, Funct, Genet , vol.23 , pp. 387-397
    • Jones, D.T.1    Miller, R.T.2    Thornton, J.M.3
  • 40
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss pdb viewer: An environment for comparative protein modelling
    • Guex N, Peitsch MC. SWISS-MODEL and the Swiss pdb viewer: An environment for comparative protein modelling. Electrophoresis 1997; 18: 2714-23.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 42
    • 0035789518 scopus 로고    scopus 로고
    • GROMACS 3.0: A package for molecular simulation and trajectory analysis
    • Lindahl E, Hess B, Van der Spoel D. GROMACS 3.0: A package for molecular simulation and trajectory analysis. J Mol Mod 2001; 7: 306-17.
    • (2001) J Mol Mod , vol.7 , pp. 306-317
    • Lindahl, E.1    Hess, B.2    Van Der Spoel, D.3
  • 43
    • 0030158429 scopus 로고    scopus 로고
    • PRODRG, a program for generating molecular toplogies and unique molecular descriptors from coordinates of small molecules
    • Van Aalten DMF, Bywater R, Findlay JBC, Hendlich M, Hooft RWW, Vriend G. PRODRG, a program for generating molecular toplogies and unique molecular descriptors from coordinates of small molecules. J Comput Aided Mol Des 1996; 10: 255-62.
    • (1996) J Comput Aided Mol Des , vol.10 , pp. 255-262
    • Van Aalten, D.M.F.1    Bywater, R.2    Findlay, J.B.C.3    Hendlich, M.4    Hooft, R.W.W.5    Vriend, G.6
  • 44
    • 0000243829 scopus 로고
    • Procheck: A program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur MW, Moss DS, hornton JM. Procheck: A program to check the stereochemical quality of protein structures. J Appl Crystallogr 1993; 26: 283-91.
    • (1993) J Appl Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Hornton, J.M.4
  • 46
    • 0025830469 scopus 로고
    • A method to identify protein sequences that fold into a known three-dimensional structure
    • Bowie JU, Luthy R, Eisenberg D. A method to identify protein sequences that fold into a known three-dimensional structure. Science 1991; 253: 164-70.
    • (1991) Science , vol.253 , pp. 164-170
    • Bowie, J.U.1    Luthy, R.2    Eisenberg, D.3
  • 47
    • 0026610767 scopus 로고
    • Assessment of protein models with three-dimensional profiles
    • Luthy R, Bowie JU, Eisenberg D. Assessment of protein models with three-dimensional profiles. Nature 1992; 356: 83-85.
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 48
    • 0025269891 scopus 로고
    • A novel method for the rapid evaluation of packing in protein structures
    • Gregoret LM, Cohen FE. A novel method for the rapid evaluation of packing in protein structures. J Mol Biol 1990; 211: 959-74.
    • (1990) J Mol Biol , vol.211 , pp. 959-974
    • Gregoret, L.M.1    Cohen, F.E.2
  • 49
    • 3042988525 scopus 로고
    • Conformational analysis 130. MM2. A hydrocarbon force field utilizing v1 and v2 torsional terms
    • Allinger NL. Conformational analysis 130. MM2. A hydrocarbon force field utilizing v1 and v2 torsional terms. J Am Chem Soc 1977; 99: 8127-34.
    • (1977) J Am Chem Soc , vol.99 , pp. 8127-8134
    • Allinger, N.L.1
  • 50
    • 33847087937 scopus 로고
    • Grond states of molecules.39.MNDO results for molecules containing hydrogen, carbon, nitrogen and oxygen
    • Dewar MJS, Thiel W. Grond states of molecules.39.MNDO results for molecules containing hydrogen, carbon, nitrogen and oxygen. J Am Chem Soc 1977; 99: 4907-17.
    • (1977) J Am Chem Soc , vol.99 , pp. 4907-4917
    • Dewar, M.J.S.1    Thiel, W.2
  • 51
    • 0028854034 scopus 로고
    • Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation
    • Jones G, Willett P, Glen RC. Molecular recognition of receptor sites using a genetic algorithm with a description of desolvation. J Mol Biol 1995; 245: 43-53.
    • (1995) J Mol Biol , vol.245 , pp. 43-53
    • Jones, G.1    Willett, P.2    Glen, R.C.3
  • 53
    • 0023759007 scopus 로고
    • The hypothetical active site lattice. An approach to modelling active sites from data on inhibitor molecules
    • Doweyko AM. The hypothetical active site lattice. An approach to modelling active sites from data on inhibitor molecules. J Med Chem 1988; 31: 1396-406.
    • (1988) J Med Chem , vol.31 , pp. 1396-1406
    • Doweyko, A.M.1
  • 54
    • 0026786837 scopus 로고
    • An application of 3D-QSAR to the analysis of the sequence specifity of DNA alkylation by uracil mustard
    • Doweyko AM, Mattes WB. An application of 3D-QSAR to the analysis of the sequence specifity of DNA alkylation by uracil mustard. Biochemistry 1992; 31: 9388-92.
    • (1992) Biochemistry , vol.31 , pp. 9388-9392
    • Doweyko, A.M.1    Mattes, W.B.2
  • 55
    • 0028362672 scopus 로고
    • Three-Dimensional pharmacophores from binding data
    • Doweyko AM. Three-Dimensional pharmacophores from binding data. J Med Chem 1994; 37: 1769-78.
    • (1994) J Med Chem , vol.37 , pp. 1769-1778
    • Doweyko, A.M.1
  • 56
    • 84986519235 scopus 로고
    • Parametrization and evaluation of a flexible water model
    • Ferguson DM. Parametrization and evaluation of a flexible water model. J Comput Chem 1995; 16: 501-11.
    • (1995) J Comput Chem , vol.16 , pp. 501-511
    • Ferguson, D.M.1
  • 57
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983; 22: 2577-637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 59
    • 0031560777 scopus 로고    scopus 로고
    • Contact area difference (CAD): A robust measure to evaluate accuracy of protein models
    • Abagyan RA, Totrov MM. Contact area difference (CAD): a robust measure to evaluate accuracy of protein models. J Mol Biol 1997; 268: 678-85.
    • (1997) J Mol Biol , vol.268 , pp. 678-685
    • Abagyan, R.A.1    Totrov, M.M.2


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