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Volumn 37, Issue 1, 2009, Pages 178-186

Human flavin-containing monooxygenase 2.1 catalyzes oxygenation of the antitubercular drugs thiacetazone and ethionamide

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; CYANAMIDE; DIMETHYLANILINE MONOOXYGENASE; DIMETHYLANILINE MONOOXYGENASE 2.1; DRUG METABOLITE; ETHIONAMIDE; QUERCETIN; SULFENIC ACID DERIVATIVE; SULFINIC ACID DERIVATIVE; THIOACETAZONE; TUBERCULOSTATIC AGENT; UNCLASSIFIED DRUG;

EID: 58149458151     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.108.024158     Document Type: Article
Times cited : (37)

References (40)
  • 3
    • 0027128951 scopus 로고
    • Cheap TB drug 'too dangerous' for Africa
    • Brown P (1992) Cheap TB drug 'too dangerous' for Africa. New Sci 135:5.
    • (1992) New Sci , vol.135 , pp. 5
    • Brown, P.1
  • 6
    • 0026611401 scopus 로고
    • Covalent binding of 14C- and 35S-labeled thiocarbamides in rat hepatic microsomes
    • Decker CJ and Doerge DR (1992) Covalent binding of 14C- and 35S-labeled thiocarbamides in rat hepatic microsomes. Biochem Pharmacol 43:881-888.
    • (1992) Biochem Pharmacol , vol.43 , pp. 881-888
    • Decker, C.J.1    Doerge, D.R.2
  • 7
    • 0021141593 scopus 로고
    • Spectrophotometric assay of the flavin-containing monooxygenase and changes in its activity in female mouse liver with nutritional and diurnal conditions
    • Dixit A and Roche TE (1984) Spectrophotometric assay of the flavin-containing monooxygenase and changes in its activity in female mouse liver with nutritional and diurnal conditions. Arch Biochem Biophys 233:50-63.
    • (1984) Arch Biochem Biophys , vol.233 , pp. 50-63
    • Dixit, A.1    Roche, T.E.2
  • 9
    • 0032515069 scopus 로고    scopus 로고
    • The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a Truncated, nonfunctional protein
    • Dolphin CT, Beckett DJ, Janmohamed A, Cullingford TE, Smith RL, Shephard EA, and Phillips LR (1998) The flavin-containing monooxygenase 2 gene (FMO2) of humans, but not of other primates, encodes a Truncated, nonfunctional protein. J Biol Chem 273:30599-30607.
    • (1998) J Biol Chem , vol.273 , pp. 30599-30607
    • Dolphin, C.T.1    Beckett, D.J.2    Janmohamed, A.3    Cullingford, T.E.4    Smith, R.L.5    Shephard, E.A.6    Phillips, L.R.7
  • 10
    • 0030063145 scopus 로고    scopus 로고
    • Differential developmental and tissue-specific regulation of expression of the genes encoding three members of the flavin-containing monooxygenase family of man, FMO1, FMO3 and FM04
    • Dolphin CT, Cullingford TE, Shephard EA, Smith RL, and Phillips IR (1996) Differential developmental and tissue-specific regulation of expression of the genes encoding three members of the flavin-containing monooxygenase family of man, FMO1, FMO3 and FM04. Eur J Biochem 235:683-689.
    • (1996) Eur J Biochem , vol.235 , pp. 683-689
    • Dolphin, C.T.1    Cullingford, T.E.2    Shephard, E.A.3    Smith, R.L.4    Phillips, I.R.5
  • 11
    • 0030667523 scopus 로고    scopus 로고
    • Missense mutation in flavin-containing mono-oxygenase 3 gene, FMO3, underlies fish-odour syndrome
    • Dolphin CT, Janmohamed A, Smith RL, Shephard EA, and Phillips IR (1997) Missense mutation in flavin-containing mono-oxygenase 3 gene, FMO3, underlies fish-odour syndrome. Nat Genet 17:491-494.
    • (1997) Nat Genet , vol.17 , pp. 491-494
    • Dolphin, C.T.1    Janmohamed, A.2    Smith, R.L.3    Shephard, E.A.4    Phillips, I.R.5
  • 13
    • 2442686708 scopus 로고    scopus 로고
    • Human flavin-containing monooxygenase form 2 S-oxygenation: Sulfenic acid formation from thioureas and oxidation of glutathione
    • Henderson MC, Krueger SK, Stevens JF, and Williams DE (2004) Human flavin-containing monooxygenase form 2 S-oxygenation: sulfenic acid formation from thioureas and oxidation of glutathione. Chem Res Toxicol 17:633-640.
    • (2004) Chem Res Toxicol , vol.17 , pp. 633-640
    • Henderson, M.C.1    Krueger, S.K.2    Stevens, J.F.3    Williams, D.E.4
  • 14
    • 1342309263 scopus 로고    scopus 로고
    • Organization and evolution of the flavin-containing monooxygenase genes of human and mouse: Identification of novel gene and pseudogene clusters
    • Hernandez D, Janmohamed A, Chandan P, Phillips IR, and Shephard EA (2004) Organization and evolution of the flavin-containing monooxygenase genes of human and mouse: identification of novel gene and pseudogene clusters. Pharmacogenetics 14:117-130.
    • (2004) Pharmacogenetics , vol.14 , pp. 117-130
    • Hernandez, D.1    Janmohamed, A.2    Chandan, P.3    Phillips, I.R.4    Shephard, E.A.5
  • 16
    • 0029132122 scopus 로고
    • Adverse cutaneous reactions to thiacetazone for tuberculosis treatment in Tanzania
    • Ipuge YA, Rieder HL, and Enarson DA (1995) Adverse cutaneous reactions to thiacetazone for tuberculosis treatment in Tanzania. Lancet 346:657-660.
    • (1995) Lancet , vol.346 , pp. 657-660
    • Ipuge, Y.A.1    Rieder, H.L.2    Enarson, D.A.3
  • 17
    • 0035885281 scopus 로고    scopus 로고
    • Quantification and cellular localization of expression in human skin of genes encoding flavin-containing monooxygenases and cytochromes P450
    • Janmohamed A, Dolphin CT, Phillips IR, and Shephard EA (2001) Quantification and cellular localization of expression in human skin of genes encoding flavin-containing monooxygenases and cytochromes P450. Biochem Pharmacol 62:777-786.
    • (2001) Biochem Pharmacol , vol.62 , pp. 777-786
    • Janmohamed, A.1    Dolphin, C.T.2    Phillips, I.R.3    Shephard, E.A.4
  • 18
    • 58149464155 scopus 로고    scopus 로고
    • Expression of recombinant flavin-containing monooxygenases in a baculovirus/insect cell system
    • Phillips IR and Shephard EA eds ed 2, pp
    • Janmohamed A, Thaunsukon P, Shephard EA, and Phillips R (2006) Expression of recombinant flavin-containing monooxygenases in a baculovirus/insect cell system, in Cytochrome P450 Protocols (Phillips IR and Shephard EA eds) ed 2, pp 307-319,
    • (2006) Cytochrome P450 Protocols , pp. 307-319
    • Janmohamed, A.1    Thaunsukon, P.2    Shephard, E.A.3    Phillips, R.4
  • 19
    • 23044469807 scopus 로고    scopus 로고
    • Discovery of novel flavin-containing monooxygenase 3 (FMO3) single nucleotide polymorphisms and functional analysis of upstream haplotype variants
    • Humana Press Totowa, NJ. Koukouritaki SB, Poch MT, Cabacungan ET, McCarver DG, and Hines RN (2005) Discovery of novel flavin-containing monooxygenase 3 (FMO3) single nucleotide polymorphisms and functional analysis of upstream haplotype variants. Mol Pharmacol 68:383-392.
    • (2005) Mol Pharmacol , vol.68 , pp. 383-392
    • Humana Press Totowa, N.J.1    Koukouritaki, S.B.2    Poch, M.T.3    Cabacungan, E.T.4    McCarver, D.G.5    Hines, R.N.6
  • 20
    • 0036157094 scopus 로고    scopus 로고
    • Human hepatic flavin-containing monooxygenases 1 (FMO1) and 3 (FMO3) developmental expression
    • Koukouritaki SB, Simpson P, Yeung CK, Rettie AE, and Hines RN (2002) Human hepatic flavin-containing monooxygenases 1 (FMO1) and 3 (FMO3) developmental expression. Pediatr Res 51:236-243.
    • (2002) Pediatr Res , vol.51 , pp. 236-243
    • Koukouritaki, S.B.1    Simpson, P.2    Yeung, C.K.3    Rettie, A.E.4    Hines, R.N.5
  • 21
    • 0021125391 scopus 로고
    • Increased biliary GSSG efflux from rat livers perfused with thiocarbamide substrates for the flavin-containing monooxygenases
    • Krieter PA, Ziegler DM, Hill KE, and Burk RF (1984) Increased biliary GSSG efflux from rat livers perfused with thiocarbamide substrates for the flavin-containing monooxygenases. Mol Pharmacol 26:122-127.
    • (1984) Mol Pharmacol , vol.26 , pp. 122-127
    • Krieter, P.A.1    Ziegler, D.M.2    Hill, K.E.3    Burk, R.F.4
  • 22
    • 0036136926 scopus 로고    scopus 로고
    • Identification of active flavin-containing monooxygenase isoform 2 in human lung and characterization of expressed protein
    • Krueger SK, Martin SR, Yueh MF, Pereira CB, and Williams DE (2002) Identification of active flavin-containing monooxygenase isoform 2 in human lung and characterization of expressed protein. Drug Metab Dispos 30:34-41.
    • (2002) Drug Metab Dispos , vol.30 , pp. 34-41
    • Krueger, S.K.1    Martin, S.R.2    Yueh, M.F.3    Pereira, C.B.4    Williams, D.E.5
  • 23
    • 19444375492 scopus 로고    scopus 로고
    • Mammalian flavin-containing monooxygenases: Structure/function, genetic polymorphisms and role in drug metabolism
    • Krueger SK and Williams DE (2005) Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism. Pharmacol Ther 106:357-387.
    • (2005) Pharmacol Ther , vol.106 , pp. 357-387
    • Krueger, S.K.1    Williams, D.E.2
  • 24
    • 0037974644 scopus 로고    scopus 로고
    • Two new polymorphisms of the FMO3 gene in Caucasian and African-American populations: Comparative genetic and functional studies
    • Lattard V, Zhang J, Tran Q, Furnes B, Schlenk D, and Cashman JR (2003) Two new polymorphisms of the FMO3 gene in Caucasian and African-American populations: comparative genetic and functional studies. Drug Metab Dispos 31:854-860.
    • (2003) Drug Metab Dispos , vol.31 , pp. 854-860
    • Lattard, V.1    Zhang, J.2    Tran, Q.3    Furnes, B.4    Schlenk, D.5    Cashman, J.R.6
  • 25
    • 0025887496 scopus 로고
    • Properties of expressed and native flavin-containing monooxygenases: Evidence of multiple forms in rabbit liver and lung
    • Lawton MP, Kronbach T, Johnson EF, and Philpot RM (1991) Properties of expressed and native flavin-containing monooxygenases: evidence of multiple forms in rabbit liver and lung. Mol Pharmacol 40:692-698.
    • (1991) Mol Pharmacol , vol.40 , pp. 692-698
    • Lawton, M.P.1    Kronbach, T.2    Johnson, E.F.3    Philpot, R.M.4
  • 26
    • 1442274747 scopus 로고    scopus 로고
    • Comparative cytotoxicity of N-substituted N′-(4-imidazole-ethyl)thiourea in precision-cut rat liver slices
    • Onderwater RC, Commandeur JN, and Vermeulen NP (2004) Comparative cytotoxicity of N-substituted N′-(4-imidazole-ethyl)thiourea in precision-cut rat liver slices. Toxicology 197: 81-91.
    • (2004) Toxicology , vol.197 , pp. 81-91
    • Onderwater, R.C.1    Commandeur, J.N.2    Vermeulen, N.P.3
  • 27
    • 33746844053 scopus 로고    scopus 로고
    • Bioactivation of N-substituted N′-(4-imidazole-ethyl)thioureas by human FMO1 and FMO3
    • Onderwater RC, Rettie AE, Commandeur JN, and Vermeulen NP (2006) Bioactivation of N-substituted N′-(4-imidazole-ethyl)thioureas by human FMO1 and FMO3. Xenobiotica 36: 645-657.
    • (2006) Xenobiotica , vol.36 , pp. 645-657
    • Onderwater, R.C.1    Rettie, A.E.2    Commandeur, J.N.3    Vermeulen, N.P.4
  • 28
    • 0027454006 scopus 로고
    • Pharmacology of the antimycobacterial drugs
    • Peloquin CA (1993) Pharmacology of the antimycobacterial drugs. Med Clin North Am 77: 1253-1262.
    • (1993) Med Clin North Am , vol.77 , pp. 1253-1262
    • Peloquin, C.A.1
  • 30
    • 37249028167 scopus 로고    scopus 로고
    • The flavin-containing monooxygenases (FMOs): Genetic variation and its consequences for the metabolism of therapeutic drugs
    • Phillips IR, Francois AA, and Shephard EA (2007) The flavin-containing monooxygenases (FMOs): Genetic variation and its consequences for the metabolism of therapeutic drugs. Current Pharmacogenomics 5:292-313.
    • (2007) Current Pharmacogenomics , vol.5 , pp. 292-313
    • Phillips, I.R.1    Francois, A.A.2    Shephard, E.A.3
  • 31
    • 44549087470 scopus 로고    scopus 로고
    • Flavin-containing monooxygenases: Mutations, disease and drug response
    • Phillips IR and Shephard EA (2008) Flavin-containing monooxygenases: mutations, disease and drug response. Trends Pharmacol Sci 29:294-301.
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 294-301
    • Phillips, I.R.1    Shephard, E.A.2
  • 32
    • 33645471799 scopus 로고    scopus 로고
    • Oxidative activation of thiacetazone by the Mycobacterium tuberculosis flavin monooxygenase EtaA and human FMO1 and FMO3
    • Qian L and Ortiz de Montellano PR (2006) Oxidative activation of thiacetazone by the Mycobacterium tuberculosis flavin monooxygenase EtaA and human FMO1 and FMO3. Chem Res Toxicol 19:443-449.
    • (2006) Chem Res Toxicol , vol.19 , pp. 443-449
    • Qian, L.1    Ortiz de Montellano, P.R.2
  • 33
    • 0036609143 scopus 로고    scopus 로고
    • Thiourea toxicity in mouse C3H/10T1/2 cells expressing human flavin-dependent monooxygenase 3
    • Smith PB and Crespi C (2002) Thiourea toxicity in mouse C3H/10T1/2 cells expressing human flavin-dependent monooxygenase 3. Biochem Pharmacol 63:1941-1948.
    • (2002) Biochem Pharmacol , vol.63 , pp. 1941-1948
    • Smith, P.B.1    Crespi, C.2
  • 34
    • 0034531789 scopus 로고    scopus 로고
    • Benzydamine N-oxidation as an index reaction reflecting FMO activity in human liver microsomes and impact of FMO3 polymorphisms on enzyme activity
    • StörmerE, Roots I, and Brockmöller J (2000) Benzydamine N-oxidation as an index reaction reflecting FMO activity in human liver microsomes and impact of FMO3 polymorphisms on enzyme activity. Br J Clin Pharmacol 50:553-561.
    • (2000) Br J Clin Pharmacol , vol.50 , pp. 553-561
    • Störmer, E.1    Roots, I.2    Brockmöller, J.3
  • 35
    • 0017096160 scopus 로고
    • Gastrointestinal toxicity of thiacetazone
    • Teklu B (1976) Gastrointestinal toxicity of thiacetazone. Ethiop Med J 14:17-22.
    • (1976) Ethiop Med J , vol.14 , pp. 17-22
    • Teklu, B.1
  • 36
    • 0037066702 scopus 로고    scopus 로고
    • The antituberculosis drug ethionamide is activated by a flavoprotein monooxygenase
    • Vannelli TA, Dykman A, and Ortiz de Montellano PR (2002) The antituberculosis drug ethionamide is activated by a flavoprotein monooxygenase. J Biol Chem 277:12824-12829.
    • (2002) J Biol Chem , vol.277 , pp. 12824-12829
    • Vannelli, T.A.1    Dykman, A.2    Ortiz de Montellano, P.R.3
  • 39
    • 0033844080 scopus 로고    scopus 로고
    • Immunoquantitation of FMO1 in human liver, kidney, and intestine
    • Yeung CK, Lang DH, Thummel KE, and Rettie AE (2000) Immunoquantitation of FMO1 in human liver, kidney, and intestine. Drag Metab Dispos 28:1107-1111.
    • (2000) Drag Metab Dispos , vol.28 , pp. 1107-1111
    • Yeung, C.K.1    Lang, D.H.2    Thummel, K.E.3    Rettie, A.E.4
  • 40
    • 0036036854 scopus 로고    scopus 로고
    • An overview of the mechanism, substrate specificities, and structure of FMOs
    • Ziegler DM (2002) An overview of the mechanism, substrate specificities, and structure of FMOs. Drug Metab Rev 34:503-511.
    • (2002) Drug Metab Rev , vol.34 , pp. 503-511
    • Ziegler, D.M.1


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