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Volumn 11, Issue 10, 2015, Pages 779-783

Structural insights into xenobiotic and inhibitor binding to human aldehyde oxidase

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE OXIDASE; PHTHALAZINE DERIVATIVE; THIORIDAZINE; XENOBIOTIC AGENT; ALDEHYDE DEHYDROGENASE; AOX1 PROTEIN, HUMAN; AOX3 PROTEIN, MOUSE; ENZYME INHIBITOR; PROTEIN BINDING;

EID: 84941876920     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.1895     Document Type: Article
Times cited : (83)

References (43)
  • 1
    • 76249096555 scopus 로고    scopus 로고
    • The mammalian aldehyde oxidase gene family
    • Garattini, E., Fratelli, M. & Terao, M. The mammalian aldehyde oxidase gene family. Hum. Genomics 4, 119-130 (2009).
    • (2009) Hum. Genomics , vol.4 , pp. 119-130
    • Garattini, E.1    Fratelli, M.2    Terao, M.3
  • 2
    • 42449117257 scopus 로고    scopus 로고
    • Mammalian aldehyde oxidases: Genetics, evolution and biochemistry
    • Garattini, E., Fratelli, M. & Terao, M. Mammalian aldehyde oxidases: genetics, evolution and biochemistry. Cell. Mol. Life Sci. 65, 1019-1048 (2008).
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 1019-1048
    • Garattini, E.1    Fratelli, M.2    Terao, M.3
  • 3
    • 84897972583 scopus 로고    scopus 로고
    • The mononuclear molybdenum enzymes
    • Hille, R., Hall, J. & Basu, P. The mononuclear molybdenum enzymes. Chem. Rev. 114, 3963-4038 (2014).
    • (2014) Chem. Rev. , vol.114 , pp. 3963-4038
    • Hille, R.1    Hall, J.2    Basu, P.3
  • 4
    • 0037954564 scopus 로고    scopus 로고
    • Mammalian molybdo-flavoenzymes, an expanding family of proteins: Structure, genetics, regulation, function and pathophysiology
    • Garattini, E., Mendel, R., Romao, M.J., Wright, R. & Terao, M. Mammalian molybdo-flavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology. Biochem. J. 372, 15-32 (2003).
    • (2003) Biochem. J. , vol.372 , pp. 15-32
    • Garattini, E.1    Mendel, R.2    Romao, M.J.3    Wright, R.4    Terao, M.5
  • 5
    • 84892737588 scopus 로고    scopus 로고
    • Identification of crucial amino acids in mouse aldehyde oxidase 3 that determine substrate specificity
    • Mahro, M. et al. Identification of crucial amino acids in mouse aldehyde oxidase 3 that determine substrate specificity. PLoS ONE 8, e82285 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e82285
    • Mahro, M.1
  • 6
    • 0020478588 scopus 로고
    • Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases
    • Wahl, R.C. & Rajagopalan, K.V. Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases. J. Biol. Chem. 257, 1354-1359 (1982).
    • (1982) J. Biol. Chem. , vol.257 , pp. 1354-1359
    • Wahl, R.C.1    Rajagopalan, K.V.2
  • 7
    • 2542612969 scopus 로고    scopus 로고
    • The crystal structure of xanthine oxidoreductase during catalysis: Implications for reaction mechanism and enzyme inhibition
    • Okamoto, K. et al. The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition. Proc. Natl. Acad. Sci. USA 101, 7931-7936 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7931-7936
    • Okamoto, K.1
  • 8
    • 17244368599 scopus 로고    scopus 로고
    • Freeze-quench magnetic circular dichroism spectroscopic study of the "very rapid" intermediate in xanthine oxidase
    • Jones, R.M., Inscore, F.E., Hille, R. & Kirk, M.L. Freeze-quench magnetic circular dichroism spectroscopic study of the "very rapid" intermediate in xanthine oxidase. Inorg. Chem. 38, 4963-4970 (1999).
    • (1999) Inorg. Chem. , vol.38 , pp. 4963-4970
    • Jones, R.M.1    Inscore, F.E.2    Hille, R.3    Kirk, M.L.4
  • 9
    • 33745871580 scopus 로고    scopus 로고
    • Avian and canine aldehyde oxidases. Novel insights into the biology and evolution of molybdo-flavoenzymes
    • Terao, M. et al. Avian and canine aldehyde oxidases. Novel insights into the biology and evolution of molybdo-flavoenzymes. J. Biol. Chem. 281, 19748-19761 (2006).
    • (2006) J. Biol. Chem. , vol.281 , pp. 19748-19761
    • Terao, M.1
  • 12
    • 78650379608 scopus 로고    scopus 로고
    • Aldehyde oxidase: An enzyme of emerging importance in drug discovery
    • Pryde, D.C. et al. Aldehyde oxidase: an enzyme of emerging importance in drug discovery. J. Med. Chem. 53, 8441-8460 (2010).
    • (2010) J. Med. Chem. , vol.53 , pp. 8441-8460
    • Pryde, D.C.1
  • 13
    • 79960719085 scopus 로고    scopus 로고
    • Increasing recognition of the importance of aldehyde oxidase in drug development and discovery
    • Garattini, E. & Terao, M. Increasing recognition of the importance of aldehyde oxidase in drug development and discovery. Drug Metab. Rev. 43, 374-386 (2011).
    • (2011) Drug Metab. Rev. , vol.43 , pp. 374-386
    • Garattini, E.1    Terao, M.2
  • 14
  • 15
    • 84884692206 scopus 로고    scopus 로고
    • Aldehyde oxidase 1 (AOX1) in human liver cytosols: Quantitative characterization of AOX1 expression level and activity relationship
    • Fu, C. et al. Aldehyde oxidase 1 (AOX1) in human liver cytosols: quantitative characterization of AOX1 expression level and activity relationship. Drug Metab. Dispos. 41, 1797-1804 (2013).
    • (2013) Drug Metab. Dispos. , vol.41 , pp. 1797-1804
    • Fu, C.1
  • 16
    • 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, M.R., Smith, J.A., Clarke, S.E. & Beedham, C. In vitro oxidation of famciclovir and 6-deoxypenciclovir by aldehyde oxidase from human, guinea pig, rabbit, and rat liver. Drug Metab. Dispos. 25, 805-813 (1997).
    • (1997) Drug Metab. Dispos. , vol.25 , pp. 805-813
    • Rashidi, M.R.1    Smith, J.A.2    Clarke, S.E.3    Beedham, C.4
  • 17
    • 0030772328 scopus 로고    scopus 로고
    • The role of non-P450 enzymes in drug oxidation
    • Beedham, C. The role of non-P450 enzymes in drug oxidation. Pharm. World Sci. 19, 255-263 (1997).
    • (1997) Pharm. World Sci. , vol.19 , pp. 255-263
    • Beedham, C.1
  • 19
    • 84870012251 scopus 로고    scopus 로고
    • The first mammalian aldehyde oxidase crystal structure: Insights into substrate specificity
    • Coelho, C. et al. The first mammalian aldehyde oxidase crystal structure: insights into substrate specificity. J. Biol. Chem. 287, 40690-40702 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 40690-40702
    • Coelho, C.1
  • 20
    • 80053139530 scopus 로고    scopus 로고
    • Characterization and crystallization of mouse aldehyde oxidase 3: From mouse liver to Escherichia coli heterologous protein expression
    • Mahro, M. et al. Characterization and crystallization of mouse aldehyde oxidase 3: from mouse liver to Escherichia coli heterologous protein expression. Drug Metab. Dispos. 39, 1939-1945 (2011).
    • (2011) Drug Metab. Dispos. , vol.39 , pp. 1939-1945
    • Mahro, M.1
  • 21
    • 27944458398 scopus 로고    scopus 로고
    • Drugs that inhibit oxidation reactions catalyzed by aldehyde oxidase do not inhibit the reductive metabolism of ziprasidone to its major metabolite, S-methyldihydroziprasidone: An in vitro study
    • Obach, R.S. & Walsky, R.L. Drugs that inhibit oxidation reactions catalyzed by aldehyde oxidase do not inhibit the reductive metabolism of ziprasidone to its major metabolite, S-methyldihydroziprasidone: an In vitro study. J. Clin. Psychopharmacol. 25, 605-608 (2005).
    • (2005) J. Clin. Psychopharmacol. , vol.25 , pp. 605-608
    • Obach, R.S.1    Walsky, R.L.2
  • 22
    • 13444256336 scopus 로고    scopus 로고
    • Antibacterial property of the antipsychotic agent prochlorperazine, and its synergism with methdilazine
    • Rani Basu, L., Mazumdar, K., Dutta, N.K., Karak, P. & Dastidar, S.G. Antibacterial property of the antipsychotic agent prochlorperazine, and its synergism with methdilazine. Microbiol. Res. 160, 95-100 (2005).
    • (2005) Microbiol. Res. , vol.160 , pp. 95-100
    • Rani Basu, L.1    Mazumdar, K.2    Dutta, N.K.3    Karak, P.4    Dastidar, S.G.5
  • 23
    • 84859428822 scopus 로고    scopus 로고
    • Why thioridazine in combination with antibiotics cures extensively drug-resistant Mycobacterium tuberculosis infections
    • Amaral, L. & Viveiros, M. Why thioridazine in combination with antibiotics cures extensively drug-resistant Mycobacterium tuberculosis infections. Int. J. Antimicrob. Agents 39, 376-380 (2012).
    • (2012) Int. J. Antimicrob. Agents , vol.39 , pp. 376-380
    • Amaral, L.1    Viveiros, M.2
  • 24
    • 84874672901 scopus 로고    scopus 로고
    • A comparative analysis of in vitro and in vivo efficacies of the enantiomers of thioridazine and its racemate
    • Christensen, J.B. et al. A comparative analysis of In vitro and in vivo efficacies of the enantiomers of thioridazine and its racemate. PLoS ONE 8, e57493 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e57493
    • Christensen, J.B.1
  • 26
    • 84893809215 scopus 로고    scopus 로고
    • Structural basis of prion inhibition by phenothiazine compounds
    • Baral, P.K. et al. Structural basis of prion inhibition by phenothiazine compounds. Structure 22, 291-303 (2014).
    • (2014) Structure , vol.22 , pp. 291-303
    • Baral, P.K.1
  • 27
    • 84927616771 scopus 로고    scopus 로고
    • Contributions of ionic interactions and protein dynamics to cytochrome P450 2D6 (CYP2D6) substrate and inhibitor binding
    • Wang, A., Stout, C.D., Zhang, Q. & Johnson, E.F. Contributions of ionic interactions and protein dynamics to cytochrome P450 2D6 (CYP2D6) substrate and inhibitor binding. J. Biol. Chem. 290, 5092-5104 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 5092-5104
    • Wang, A.1    Stout, C.D.2    Zhang, Q.3    Johnson, E.F.4
  • 28
    • 0034718556 scopus 로고    scopus 로고
    • Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: Structure-based mechanism of conversion
    • Enroth, C., Eger, B.T., Okamoto, K., Nishino, T. & Pai, E.F. Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion. Proc. Natl. Acad. Sci. USA 97, 10723-10728 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10723-10728
    • Enroth, C.1    Eger, B.T.2    Okamoto, K.3    Nishino, T.4    Pai, E.F.5
  • 29
    • 84855943310 scopus 로고    scopus 로고
    • Protein conformational gating of enzymatic activity in xanthine oxidoreductase
    • Ishikita, H., Eger, B.T., Okamoto, K., Nishino, T. & Pai, E.F. Protein conformational gating of enzymatic activity in xanthine oxidoreductase. J. Am. Chem. Soc. 134, 999-1009 (2012).
    • (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
  • 30
    • 84884836370 scopus 로고    scopus 로고
    • Structural analysis of phenothiazine derivatives as allosteric inhibitors of the MALT1 paracaspase
    • Schlauderer, F. et al. Structural analysis of phenothiazine derivatives as allosteric inhibitors of the MALT1 paracaspase. Angew. Chem. Int. Ed. Engl. 52, 10384-10387 (2013).
    • (2013) Angew. Chem. Int. Ed. Engl. , vol.52 , pp. 10384-10387
    • Schlauderer, F.1
  • 31
    • 84857195686 scopus 로고    scopus 로고
    • In vitro screening and structural characterization of inhibitors of the S100B-p53 interaction
    • Wilder, P.T. et al. In vitro screening and structural characterization of inhibitors of the S100B-p53 interaction. Int. J. High Throughput Screen. 2010, 109-126 (2010).
    • (2010) Int. J. High Throughput Screen. , vol.2010 , pp. 109-126
    • Wilder, P.T.1
  • 32
    • 81855217400 scopus 로고    scopus 로고
    • Inhibition of human liver aldehyde oxidase: Implications for potential drug-drug interactions
    • Barr, J.T. & Jones, J.P. Inhibition of human liver aldehyde oxidase: implications for potential drug-drug interactions. Drug Metab. Dispos. 39, 2381-2386 (2011).
    • (2011) Drug Metab. Dispos. , vol.39 , pp. 2381-2386
    • Barr, J.T.1    Jones, J.P.2
  • 33
    • 65949088825 scopus 로고    scopus 로고
    • Molybdenum and tungsten enzymes: A crystallographic and mechanistic overview
    • Romão, M.J. Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview. Dalton Trans. 21, 4053-4068 (2009).
    • (2009) Dalton Trans. , vol.21 , pp. 4053-4068
    • Romão, M.J.1
  • 34
    • 0029882611 scopus 로고    scopus 로고
    • Involvement of the narJ and mobgene products in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli
    • Palmer, T. et al. Involvement of the narJ and mobgene products in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli. Mol. Microbiol. 20, 875-884 (1996).
    • (1996) Mol. Microbiol. , vol.20 , pp. 875-884
    • Palmer, T.1
  • 35
    • 0034669320 scopus 로고    scopus 로고
    • Optimization of expression of human sulfite oxidase and its molybdenum domain
    • Temple, C.A., Graf, T.N. & Rajagopalan, K.V. Optimization of expression of human sulfite oxidase and its molybdenum domain. Arch. Biochem. Biophys. 383, 281-287 (2000).
    • (2000) Arch. Biochem. Biophys. , vol.383 , pp. 281-287
    • Temple, C.A.1    Graf, T.N.2    Rajagopalan, K.V.3
  • 36
    • 84859917371 scopus 로고    scopus 로고
    • The impact of single nucleotide polymorphisms on human aldehyde oxidase
    • Hartmann, T. et al. The impact of single nucleotide polymorphisms on human aldehyde oxidase. Drug Metab. Dispos. 40, 856-864 (2012).
    • (2012) Drug Metab. Dispos. , vol.40 , pp. 856-864
    • Hartmann, T.1


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