메뉴 건너뛰기




Volumn 34, Issue 12, 2006, Pages 1995-2002

Investigation of structure and function of a catalytically efficient variant of the human flavin-containing monooxygenase form 3

Author keywords

[No Author keywords available]

Indexed keywords

10 [(N,N, DIMETHYLAMINOPENTYL) 2 (TRIFLUOROMETHYL)]PHENOTHIAZINE; CHLORPROMAZINE; DIMETHYLANILINE MONOOXYGENASE; FLAVIN CONTAINING MONOOXYGENASE 1; FLAVIN CONTAINING MONOOXYGENASE 3; IMIDAZOLE DERIVATIVE; MERCAPTOIMIDAZOLE; PHENOTHIAZINE DERIVATIVE;

EID: 33751535481     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.106.010827     Document Type: Article
Times cited : (13)

References (46)
  • 2
    • 27544432463 scopus 로고    scopus 로고
    • Dynamics involved in catalysis by single-component and two-component flavin-dependent aromatic hydroxylases
    • Ballou DP, Entsch B, and Cole LJ (2005) Dynamics involved in catalysis by single-component and two-component flavin-dependent aromatic hydroxylases. Biochem Biophys Res Commun 338:590-598.
    • (2005) Biochem Biophys Res Commun , vol.338 , pp. 590-598
    • Ballou, D.P.1    Entsch, B.2    Cole, L.J.3
  • 3
    • 19444377980 scopus 로고
    • A kinetic investigation of liver microsomal mixed function amine oxidase
    • (Coon MJ, Conney AH, Estabrook RW, Gelboin HV, Gillette JR, and O'Brien PJ eds) Academic Press, New York
    • Beaty N and Ballou D (1980) A kinetic investigation of liver microsomal mixed function amine oxidase, in Microsomes, Drug Oxidation and Chemical Carcinogenesis, (Coon MJ, Conney AH, Estabrook RW, Gelboin HV, Gillette JR, and O'Brien PJ eds) pp 209-302, Academic Press, New York.
    • (1980) Microsomes, Drug Oxidation and Chemical Carcinogenesis , pp. 209-302
    • Beaty, N.1    Ballou, D.2
  • 5
    • 0030803384 scopus 로고    scopus 로고
    • Characterization of two human flavin-containing monooxygenase (form 3) enzymes expressed in Escherichia coli as maltose binding protein fusions
    • Brunelle A, Bi YA, Lin J, Russell B, Luy L, Berkman C, and Cashman J (1997) Characterization of two human flavin-containing monooxygenase (form 3) enzymes expressed in Escherichia coli as maltose binding protein fusions. Drug Metab Dispos 25:1001-1007.
    • (1997) Drug Metab Dispos , vol.25 , pp. 1001-1007
    • Brunelle, A.1    Bi, Y.A.2    Lin, J.3    Russell, B.4    Luy, L.5    Berkman, C.6    Cashman, J.7
  • 6
    • 0028945438 scopus 로고
    • Structural and catalytic properties of the mammalian flavin-containing monooxygenase
    • Cashman JR (1995) Structural and catalytic properties of the mammalian flavin-containing monooxygenase. Chem Res Toxicol 8:165-181.
    • (1995) Chem Res Toxicol , vol.8 , pp. 165-181
    • Cashman, J.R.1
  • 7
    • 0036265797 scopus 로고    scopus 로고
    • Human flavin-containing monooxygenase (form 3): Polymorphisms and variations in chemical metabolism
    • Cashman JR (2002a) Human flavin-containing monooxygenase (form 3): polymorphisms and variations in chemical metabolism. Pharmacogenomics 3:325-339.
    • (2002) Pharmacogenomics , vol.3 , pp. 325-339
    • Cashman, J.R.1
  • 10
    • 0036786378 scopus 로고    scopus 로고
    • Interindividual differences of human flavin-containing monooxygenase 3: Genetic polymorphisms and functional variation
    • Cashman JR and Zhang J (2002) Interindividual differences of human flavin-containing monooxygenase 3: genetic polymorphisms and functional variation. Drug Metab Dispos 30:1043-1052.
    • (2002) Drug Metab Dispos , vol.30 , pp. 1043-1052
    • Cashman, J.R.1    Zhang, J.2
  • 12
    • 0035201442 scopus 로고    scopus 로고
    • Population distribution of human flavin-containing monooxygenase form 3: Gene polymorphisms
    • Cashman JR, Zhang J, Leushner J, and Braun A (2001) Population distribution of human flavin-containing monooxygenase form 3: gene polymorphisms. Drug Metab Dispos 29:1629-1637.
    • (2001) Drug Metab Dispos , vol.29 , pp. 1629-1637
    • Cashman, J.R.1    Zhang, J.2    Leushner, J.3    Braun, A.4
  • 13
    • 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
  • 14
    • 0030667523 scopus 로고    scopus 로고
    • Missense mutation in flavin-containing monooxygenase 3 gene, underlies fish-odour syndrome
    • Dolphin CT, Janmohamed A, Smith RL, Shephard EA, and Phillips IR (1997) Missense mutation in flavin-containing monooxygenase 3 gene, 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
  • 15
    • 0034523352 scopus 로고    scopus 로고
    • Compound heterozygosity for missense mutations in the flavin-containing monooxygenase 3 (FMO3) gene in patients with fish-odour syndrome
    • Dolphin CT, Janmohamed A, Smith RL, Shephard EA, and Phillips IR (2000) Compound heterozygosity for missense mutations in the flavin-containing monooxygenase 3 (FMO3) gene in patients with fish-odour syndrome. Pharmacogenetics 20:799-807.
    • (2000) Pharmacogenetics , vol.20 , pp. 799-807
    • Dolphin, C.T.1    Janmohamed, A.2    Smith, R.L.3    Shephard, E.A.4    Phillips, I.R.5
  • 17
    • 12244306252 scopus 로고    scopus 로고
    • Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans
    • Furnes B, Feng J, Sommer S, and 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.3    Schlenk, D.4
  • 18
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex N and Peitsch MC (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18:2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 19
    • 0034097599 scopus 로고    scopus 로고
    • Stereoselective sulfoxidation of sulindac sulfide by flavin-containing monooxygenases. Comparison of human liver and kidney microsomes and mammalian enzymes
    • Hamman MA, Haehner-Daniels BD, Wrighton SA, Rettie AE, and Hall SD (2000) Stereoselective sulfoxidation of sulindac sulfide by flavin-containing monooxygenases. Comparison of human liver and kidney microsomes and mammalian enzymes. Biochem Pharmacol 60:7-17.
    • (2000) Biochem Pharmacol , vol.60 , pp. 7-17
    • Hamman, M.A.1    Haehner-Daniels, B.D.2    Wrighton, S.A.3    Rettie, A.E.4    Hall, S.D.5
  • 20
    • 1342309263 scopus 로고    scopus 로고
    • Organization and evolution of the flavin-containing monooxygenase genes of human and mouse; identification of novel gene 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 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
  • 21
    • 0036076899 scopus 로고    scopus 로고
    • Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase
    • Hines RN, Hopp KA, Fanco J, Saeian K, and Begun FP (2002) Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase. Mol Pharmacol 62:320-325.
    • (2002) Mol Pharmacol , vol.62 , pp. 320-325
    • Hines, R.N.1    Hopp, K.A.2    Fanco, J.3    Saeian, K.4    Begun, F.P.5
  • 22
    • 11144226352 scopus 로고    scopus 로고
    • Genetic polymorphisms of human flavin-containing monooxygenase 3 in sulindac-mediated primary chemoprevention of familial adenomatous polyposis
    • Hisamuddin IM, Whebi MA, Chao A, Wyre HW, Hylind LM, Giardiello FM, and Yang VW (2004) Genetic polymorphisms of human flavin-containing monooxygenase 3 in sulindac-mediated primary chemoprevention of familial adenomatous polyposis. Clin Cancer Res 10:8357-8362.
    • (2004) Clin Cancer Res , vol.10 , pp. 8357-8362
    • Hisamuddin, I.M.1    Whebi, M.A.2    Chao, A.3    Wyre, H.W.4    Hylind, L.M.5    Giardiello, F.M.6    Yang, V.W.7
  • 23
    • 0034053228 scopus 로고    scopus 로고
    • Phenotypes of flavin-containing monooxygenase activity determined by ranitidine N-oxidation are positively correlated with genotypes of linked FM03 gene mutations in a Korean population
    • Kang JH, Chung WG, Lee KH, Park CS, Kang JS, Shin IC, Roh HK, Dong MS, Baek HM, and Cha YN (2000) Phenotypes of flavin-containing monooxygenase activity determined by ranitidine N-oxidation are positively correlated with genotypes of linked FM03 gene mutations in a Korean population. Pharmacogenetics 10:67-78.
    • (2000) Pharmacogenetics , vol.10 , pp. 67-78
    • Kang, J.H.1    Chung, W.G.2    Lee, K.H.3    Park, C.S.4    Kang, J.S.5    Shin, I.C.6    Roh, H.K.7    Dong, M.S.8    Baek, H.M.9    Cha, Y.N.10
  • 24
    • 28444441585 scopus 로고    scopus 로고
    • Flavin-containing monooxygenase genetic polymorphism: Impact on chemical metabolism and drug development
    • Koukouritaki SB and Hines RN (2005) Flavin-containing monooxygenase genetic polymorphism: impact on chemical metabolism and drug development. Pharmacogenomics 8:807-822.
    • (2005) Pharmacogenomics , vol.8 , pp. 807-822
    • Koukouritaki, S.B.1    Hines, R.N.2
  • 25
    • 23044469807 scopus 로고    scopus 로고
    • Discovery of novel flavin-containing monooxygenase 3 (FMO3) single nucleotide polymorphisms and functional analysis of upstream haplotype variants
    • 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
    • Koukouritaki, S.B.1    Poch, M.T.2    Cabacungan, E.T.3    McCarver, D.G.4    Hines, R.N.5
  • 26
    • 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
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond) 227:680-685.
    • (1970) Nature (Lond) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 28
    • 2442642701 scopus 로고    scopus 로고
    • Alternative processing events in human FMO genes
    • Lattard V, Zhang J, and Cashman JR (2004) Alternative processing events in human FMO genes. Mol Pharmacol 65:1517-1525.
    • (2004) Mol Pharmacol , vol.65 , pp. 1517-1525
    • Lattard, V.1    Zhang, J.2    Cashman, J.R.3
  • 29
    • 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
  • 31
    • 0026501232 scopus 로고
    • Molecular cloning of flavin-containing monooxygenase (form II) cDNA from adult human liver
    • Lomri N, Gu Q, and Cashman JR (1992) Molecular cloning of flavin-containing monooxygenase (form II) cDNA from adult human liver. Proc Natl Acad Sci USA 89:1685-1689.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 1685-1689
    • Lomri, N.1    Gu, Q.2    Cashman, J.R.3
  • 32
    • 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, and Cashman JR (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.R.3
  • 34
    • 9244265499 scopus 로고    scopus 로고
    • Benzydamine metabolism in vivo is impaired in patients with deficiency of flavin-containing monooxygenase 3
    • Mayatepek E, Flock B, and Zschocke J (2004) Benzydamine metabolism in vivo is impaired in patients with deficiency of flavin-containing monooxygenase 3. Pharmacogenetics 14:775-777.
    • (2004) Pharmacogenetics , vol.14 , pp. 775-777
    • Mayatepek, E.1    Flock, B.2    Zschocke, J.3
  • 35
    • 0030897424 scopus 로고    scopus 로고
    • Studies on the discontinuous N-oxidation of trimethylamine among Jordanian, Ecuadorian and New Guinean populations
    • Mitchell SC, Zhang AQ, Barrett T, Ayesh R, and Smith RL (1997) Studies on the discontinuous N-oxidation of trimethylamine among Jordanian, Ecuadorian and New Guinean populations. Pharmacogenetics 7:45-50.
    • (1997) Pharmacogenetics , vol.7 , pp. 45-50
    • Mitchell, S.C.1    Zhang, A.Q.2    Barrett, T.3    Ayesh, R.4    Smith, R.L.5
  • 37
    • 0036152701 scopus 로고    scopus 로고
    • Ethnic differences in allelic frequency of two flavin-containing monooxygenase 3 (FMO3) polymorphisms: Linkage and effects on in vivo and in vitro FMO activities
    • Park CS, Kang JH, Chung WG, Yi HG, Pie JE, Park DK, Hines RN, McCarver DG, and Cha YN (2002) Ethnic differences in allelic frequency of two flavin-containing monooxygenase 3 (FMO3) polymorphisms: linkage and effects on in vivo and in vitro FMO activities. Pharmacogenetics 12:77-80.
    • (2002) Pharmacogenetics , vol.12 , pp. 77-80
    • Park, C.S.1    Kang, J.H.2    Chung, W.G.3    Yi, H.G.4    Pie, J.E.5    Park, D.K.6    Hines, R.N.7    McCarver, D.G.8    Cha, Y.N.9
  • 38
    • 0029004590 scopus 로고
    • Protein modeling by email
    • Peitsch MC (1995) Protein modeling by email. Bio/Technology 13:658-660.
    • (1995) Bio/Technology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 39
    • 0018801101 scopus 로고
    • The liver microsomal FAD-containing monooxygenase: Spectral characterization and kinetic studies
    • Poulsen LL and Ziegler DM (1979) The liver microsomal FAD-containing monooxygenase: spectral characterization and kinetic studies. J Biol Chem 254:6449-6455.
    • (1979) J Biol Chem , vol.254 , pp. 6449-6455
    • Poulsen, L.L.1    Ziegler, D.M.2
  • 40
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede T, Kopp J, Guex N, and Peitsch MC (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31:3381-3385.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 41
    • 0025996658 scopus 로고
    • Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 angstroms resolution
    • Stehle T, Ahmed SA, Claiborne A, and Schulz GE (1991) Structure of NADH peroxidase from Streptococcus faecalis 10C1 refined at 2.16 angstroms resolution. J Mol Biol 221:1325-1330.
    • (1991) J Mol Biol , vol.221 , pp. 1325-1330
    • Stehle, T.1    Ahmed, S.A.2    Claiborne, A.3    Schulz, G.E.4
  • 43
    • 0032574741 scopus 로고    scopus 로고
    • Identification of amino acid residues associated with modulation of flavin-containing monooxygenase (FMO) activity by imipramine: Structure/function studies with FMO1 from pig and rabbit
    • Wyatt MK, Overby LH, Lawton MP, and Philpot RM (1998) Identification of amino acid residues associated with modulation of flavin-containing monooxygenase (FMO) activity by imipramine: structure/function studies with FMO1 from pig and rabbit. Biochemistry 37:5930-5938.
    • (1998) Biochemistry , vol.37 , pp. 5930-5938
    • Wyatt, M.K.1    Overby, L.H.2    Lawton, M.P.3    Philpot, R.M.4
  • 44
    • 29944437885 scopus 로고    scopus 로고
    • Quantitative analysis of FMO gene mRNA levels in human tissues
    • Zhang J and Cashman JR (2006) Quantitative analysis of FMO gene mRNA levels in human tissues. Drug Metab Dispos 34:19-26.
    • (2006) Drug Metab Dispos , vol.34 , pp. 19-26
    • Zhang, J.1    Cashman, J.R.2
  • 45
    • 0023894686 scopus 로고
    • Flavin-containing monooxygenases: Catalytic mechanism and substrate specificities
    • Ziegler DM (1988) Flavin-containing monooxygenases: catalytic mechanism and substrate specificities. Drug Metab Rev 19:1-32.
    • (1988) Drug Metab Rev , vol.19 , pp. 1-32
    • Ziegler, D.M.1
  • 46
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.