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Volumn 14, Issue 1, 2015, Pages

Human FMO2-based microbial whole-cell catalysts for drug metabolite synthesis

Author keywords

Drug metabolites; Escherichia coli; Flavin monooxygenase isoform 2; FMO2; Propranolol; Trifluoperazine; Whole cell biocatalysis

Indexed keywords

BENZYDAMINE; BENZYDAMINE N OXIDE; CELL PROTEIN; DRUG METABOLITE; ETHIONAMIDE; ETHIONAMIDE N OXIDE; FLAVIN MONOOXYGENASE ISOFORM 2; OXIDE; TRIFLUOPERAZINE; UNCLASSIFIED DRUG; 4,6-DINITRO-O-CRESOL; DINITRO ORTHO CRESOL; DRUG; MIXED FUNCTION OXIDASE; PROPRANOLOL; RECOMBINANT PROTEIN;

EID: 84935001735     PISSN: None     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/s12934-015-0262-0     Document Type: Article
Times cited : (19)

References (33)
  • 1
    • 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 et al (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
  • 2
    • 0034329485 scopus 로고    scopus 로고
    • Ethnic differences in human flavin-containing monooxygenase 2 (FMO2) polymorphisms: detection of expressed protein in African-Americans
    • Whetstine JR, Yueh MF, McCarver DG, Williams DE, Park CS, Kang JH et al (2000) Ethnic differences in human flavin-containing monooxygenase 2 (FMO2) polymorphisms: detection of expressed protein in African-Americans. Toxicol Appl Pharmacol 168:216-224
    • (2000) Toxicol Appl Pharmacol , vol.168 , pp. 216-224
    • Whetstine, J.R.1    Yueh, M.F.2    McCarver, D.G.3    Williams, D.E.4    Park, C.S.5    Kang, J.H.6
  • 3
    • 12244306252 scopus 로고    scopus 로고
    • Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans
    • Furnes B, Feng J, Sommer SS, Schlenk D (2003) Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos 31:187-193
    • (2003) Drug Metab Dispos , vol.31 , pp. 187-193
    • Furnes, B.1    Feng, J.2    Sommer, S.S.3    Schlenk, D.4
  • 4
    • 53549126881 scopus 로고    scopus 로고
    • The potentially deleterious functional variant flavin-containing monooxygenase 2*1 is at high frequency throughout sub-Saharan Africa
    • Veeramah KR, Thomas MG, Weale ME, Zeitlyn D, Tarekegn A, Bekele E et al (2008) The potentially deleterious functional variant flavin-containing monooxygenase 2*1 is at high frequency throughout sub-Saharan Africa. Pharmacogenet Genomics 18:877-886
    • (2008) Pharmacogenet Genomics , vol.18 , pp. 877-886
    • Veeramah, K.R.1    Thomas, M.G.2    Weale, M.E.3    Zeitlyn, D.4    Tarekegn, A.5    Bekele, E.6
  • 6
    • 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, 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
  • 8
    • 58149458151 scopus 로고    scopus 로고
    • Human flavin-containing monooxygenase 2.1 catalyzes oxygenation of the antitubercular drugs thiacetazone and ethionamide
    • Francois AA, Nishida CR, De Montellano PRO, Phillips IR, Shephard EA (2009) Human flavin-containing monooxygenase 2.1 catalyzes oxygenation of the antitubercular drugs thiacetazone and ethionamide. Drug Metab Dispos 37:178-186
    • (2009) Drug Metab Dispos , vol.37 , pp. 178-186
    • Francois, A.A.1    Nishida, C.R.2    De, M.P.R.O.3    Phillips, I.R.4    Shephard, E.A.5
  • 9
    • 56249123296 scopus 로고    scopus 로고
    • Metabolism of the anti-tuberculosis drug ethionamide by mouse and human FMO1, FMO2 and FMO3 and mouse and human lung microsomes
    • Henderson MC, Siddens LK, Morré JT, Krueger SK, Williams DE (2008) Metabolism of the anti-tuberculosis drug ethionamide by mouse and human FMO1, FMO2 and FMO3 and mouse and human lung microsomes. Toxicol Appl Pharmacol 233:420-427
    • (2008) Toxicol Appl Pharmacol , vol.233 , pp. 420-427
    • Henderson, M.C.1    Siddens, L.K.2    Morré, J.T.3    Krueger, S.K.4    Williams, D.E.5
  • 10
    • 0022861737 scopus 로고
    • Substrate specificity of the rabbit lung flavin-containing monooxygenase for amines: oxidation products of primary alkylamines
    • Poulsen LL, Taylor K, Williams DE, Masters BSS, Ziegler DM (1986) Substrate specificity of the rabbit lung flavin-containing monooxygenase for amines: oxidation products of primary alkylamines. Mol Pharmacol 60:680-685
    • (1986) Mol Pharmacol , vol.60 , pp. 680-685
    • Poulsen, L.L.1    Taylor, K.2    Williams, D.E.3    Masters, B.S.S.4    Ziegler, D.M.5
  • 11
    • 0022860321 scopus 로고
    • Formation of hydrogen peroxide and N-hydroxylated amines catalyzed by pulmonary flavin-containing monooxygenases in the presence of primary alkylamines
    • Tynes RE, Sabourin PJ, Hodgson E, Philpot RM (1986) Formation of hydrogen peroxide and N-hydroxylated amines catalyzed by pulmonary flavin-containing monooxygenases in the presence of primary alkylamines. Arch Biochem Biophys 251:654-664
    • (1986) Arch Biochem Biophys , vol.251 , pp. 654-664
    • Tynes, R.E.1    Sabourin, P.J.2    Hodgson, E.3    Philpot, R.M.4
  • 13
    • 0033836020 scopus 로고    scopus 로고
    • Isoform specificity of N-deacetyl ketoconazole by human and rabbit flavin-containing monooxygenases
    • Rodriguez RJ, Miranda CL (2000) Isoform specificity of N-deacetyl ketoconazole by human and rabbit flavin-containing monooxygenases. Drug Metab Dispos 28:1083-1086
    • (2000) Drug Metab Dispos , vol.28 , pp. 1083-1086
    • Rodriguez, R.J.1    Miranda, C.L.2
  • 14
    • 62249177821 scopus 로고    scopus 로고
    • Metabolites in safety testing (MIST): considerations of mechanisms of toxicity with dose, abundance, and duration of treatment
    • Smith DA, Obach RS (2009) Metabolites in safety testing (MIST): considerations of mechanisms of toxicity with dose, abundance, and duration of treatment. Chem Res Toxicol 22:267-279
    • (2009) Chem Res Toxicol , vol.22 , pp. 267-279
    • Smith, D.A.1    Obach, R.S.2
  • 15
    • 0035424201 scopus 로고    scopus 로고
    • Using proteins in their natural environment: potential and limitations of microbial whole-cell hydroxylations in applied biocatalysis
    • Duetz WA, Van Beilen JB, Witholt B (2001) Using proteins in their natural environment: potential and limitations of microbial whole-cell hydroxylations in applied biocatalysis. Curr Opin Biotechnol 12:419-425
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 419-425
    • Duetz, W.A.1    Van, B.J.B.2    Witholt, B.3
  • 16
    • 35348890863 scopus 로고    scopus 로고
    • An efficient plasmid vector for expression cloning of large numbers of PCR fragments in Escherichia coli
    • Reisinger C, Kern A, Fesko K, Schwab H (2007) An efficient plasmid vector for expression cloning of large numbers of PCR fragments in Escherichia coli. Appl Microbiol Biotechnol 77:241-244
    • (2007) Appl Microbiol Biotechnol , vol.77 , pp. 241-244
    • Reisinger, C.1    Kern, A.2    Fesko, K.3    Schwab, H.4
  • 17
    • 0027185830 scopus 로고
    • Expression in Escherichia coli of the flavin-containing monooxygenase D (form II) from adult human liver: determination of a distinct tertiary amine substrate specificity
    • Lomri N, Yang Z, Cashman J (1993) Expression in Escherichia coli of the flavin-containing monooxygenase D (form II) from adult human liver: determination of a distinct tertiary amine substrate specificity. Chem Res Toxicol 6:425-429
    • (1993) Chem Res Toxicol , vol.6 , pp. 425-429
    • Lomri, N.1    Yang, Z.2    Cashman, J.3
  • 18
    • 0028930879 scopus 로고
    • Characterisation of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog
    • Overby LH, Buckpitt AR, Lawton MP, Atta-Asafo-Adjei E, Schulze J, Philpot RM (1995) Characterisation of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog. Arch Biochem Biophys 317:275-284
    • (1995) Arch Biochem Biophys , vol.317 , pp. 275-284
    • Overby, L.H.1    Buckpitt, A.R.2    Lawton, M.P.3    Atta-Asafo-Adjei, E.4    Schulze, J.5    Philpot, R.M.6
  • 19
    • 0031282528 scopus 로고    scopus 로고
    • Molecular cloning, sequencing, and expression in Escherichia coli of mouse flavin-containing monooxygenase 3 (FMO3): comparison with the human isoform 1
    • Falls JG, Cherrington NJ, Clements KM, Philpot RM, Levi PE, Rose RL et al (1997) Molecular cloning, sequencing, and expression in Escherichia coli of mouse flavin-containing monooxygenase 3 (FMO3): comparison with the human isoform 1. Arch Biochem Biophys 347:9-18
    • (1997) Arch Biochem Biophys , vol.347 , pp. 9-18
    • Falls, J.G.1    Cherrington, N.J.2    Clements, K.M.3    Philpot, R.M.4    Levi, P.E.5    Rose, R.L.6
  • 20
    • 84861605139 scopus 로고    scopus 로고
    • Expression of recombinant human flavin monooxygenase and moclobemide-N-oxide synthesis on multi-mg scale
    • Hanlon SP, Camattari A, Abad S, Glieder A, Kittelmann M, Lütz S et al (2012) Expression of recombinant human flavin monooxygenase and moclobemide-N-oxide synthesis on multi-mg scale. Chem Commun (Camb) 48:6001-6003
    • (2012) Chem Commun (Camb) , vol.48 , pp. 6001-6003
    • Hanlon, S.P.1    Camattari, A.2    Abad, S.3    Glieder, A.4    Kittelmann, M.5    Lütz, S.6
  • 22
    • 84855816174 scopus 로고    scopus 로고
    • In vitro drug metabolism by C-terminally truncated human flavin-containing monooxygenase 3
    • Catucci G, Gilardi G, Jeuken L, Sadeghi SJ (2012) In vitro drug metabolism by C-terminally truncated human flavin-containing monooxygenase 3. Biochem Pharmacol 83:551-558
    • (2012) Biochem Pharmacol , vol.83 , pp. 551-558
    • Catucci, G.1    Gilardi, G.2    Jeuken, L.3    Sadeghi, S.J.4
  • 23
    • 0027466902 scopus 로고
    • Functional characterization of flavin-containing monooxygenase 1B1 expressed in Saccharomyces cerevisiae and Escherichia coli and analysis of proposed FAD- and membrane-binding domains
    • Lawton MP, Philpot RM (1993) Functional characterization of flavin-containing monooxygenase 1B1 expressed in Saccharomyces cerevisiae and Escherichia coli and analysis of proposed FAD- and membrane-binding domains. J Biol Chem 268:5728-5734
    • (1993) J Biol Chem , vol.268 , pp. 5728-5734
    • Lawton, M.P.1    Philpot, R.M.2
  • 24
    • 19444375492 scopus 로고    scopus 로고
    • Mammalian flavin-containing monooxygenases: structure/function, genetic polymorphisms and role in drug metabolism
    • Krueger SK, 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
  • 25
    • 33750041365 scopus 로고    scopus 로고
    • An evaluation of the efficacy of aspirin and benzydamine hydrochloride gargle for attenuating postoperative sore throat: a prospective, randomized, single-blind study
    • Agarwal A, Nath SS, Goswami D, Gupta D, Dhiraaj S, Singh PK (2006) An evaluation of the efficacy of aspirin and benzydamine hydrochloride gargle for attenuating postoperative sore throat: a prospective, randomized, single-blind study. Anesth Analg 103:1001-1003
    • (2006) Anesth Analg , vol.103 , pp. 1001-1003
    • Agarwal, A.1    Nath, S.S.2    Goswami, D.3    Gupta, D.4    Dhiraaj, S.5    Singh, P.K.6
  • 26
    • 84878869534 scopus 로고    scopus 로고
    • Molecular and functional characterization of flavin-containing monooxygenases in cynomolgus macaque
    • Uno Y, Shimizu M, Yamazaki H (2013) Molecular and functional characterization of flavin-containing monooxygenases in cynomolgus macaque. Biochem Pharmacol 85:1837-1847
    • (2013) Biochem Pharmacol , vol.85 , pp. 1837-1847
    • Uno, Y.1    Shimizu, M.2    Yamazaki, H.3
  • 27
    • 0021747810 scopus 로고
    • Rabbit lung flavin-containing monooxygenase is immunochemically and catalytically distinct from the liver enzyme
    • Williams DE, Ziegler DM, Nordin DJ, Hale SE, Masters BSS (1984) Rabbit lung flavin-containing monooxygenase is immunochemically and catalytically distinct from the liver enzyme. Biochem Biophys Res Commun 125:116-122
    • (1984) Biochem Biophys Res Commun , vol.125 , pp. 116-122
    • Williams, D.E.1    Ziegler, D.M.2    Nordin, D.J.3    Hale, S.E.4    Masters, B.S.S.5
  • 29
    • 0028020099 scopus 로고
    • Cytochrome P450 isozymes involved in propranolol metabolism in human liver microsomes. The role of CYP2D6 as ring-hydroxylase and CYP1A2 as N-desisopropylase
    • Masubuchi Y, Hosokawa S, Horie T, Suzuki T, Ohmori S, Kitada M et al (1994) Cytochrome P450 isozymes involved in propranolol metabolism in human liver microsomes. The role of CYP2D6 as ring-hydroxylase and CYP1A2 as N-desisopropylase. Drug Metab Dispos 22:909-915
    • (1994) Drug Metab Dispos , vol.22 , pp. 909-915
    • Masubuchi, Y.1    Hosokawa, S.2    Horie, T.3    Suzuki, T.4    Ohmori, S.5    Kitada, M.6
  • 30
    • 0028956887 scopus 로고
    • Identification of human CYP isoforms involved in the metabolism of propranolol enantiomers-N-desisopropylation is mediated mainly by CYP1A2
    • Yoshimoto K, Echizen H, Chiba K, Tani M, Ishizaki T (1995) Identification of human CYP isoforms involved in the metabolism of propranolol enantiomers-N-desisopropylation is mediated mainly by CYP1A2. Br J Clin Pharmacol 39:421-431
    • (1995) Br J Clin Pharmacol , vol.39 , pp. 421-431
    • Yoshimoto, K.1    Echizen, H.2    Chiba, K.3    Tani, M.4    Ishizaki, T.5
  • 31
    • 2942585606 scopus 로고    scopus 로고
    • Porcine FAD-containing monooxygenase metabolizes lidocaine, bupivacaine and propranolol in vitro
    • Wu RF, Liao CX, Tomita S, Ichikawa Y, Terada LS (2004) Porcine FAD-containing monooxygenase metabolizes lidocaine, bupivacaine and propranolol in vitro. Life Sci 75:1011-1019
    • (2004) Life Sci , vol.75 , pp. 1011-1019
    • Wu, R.F.1    Liao, C.X.2    Tomita, S.3    Ichikawa, Y.4    Terada, L.S.5
  • 32
    • 67650348339 scopus 로고    scopus 로고
    • Evaluation of the metabolism of propranolol by linear ion trap technology in mouse, rat, dog, monkey, and human cryopreserved hepatocytes
    • Baughman TM, Talarico CL, Soglia JR (2009) Evaluation of the metabolism of propranolol by linear ion trap technology in mouse, rat, dog, monkey, and human cryopreserved hepatocytes. Rapid Commun Mass Spectrom 23:2146-2150
    • (2009) Rapid Commun Mass Spectrom , vol.23 , pp. 2146-2150
    • Baughman, T.M.1    Talarico, C.L.2    Soglia, J.R.3


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