메뉴 건너뛰기




Volumn 97, Issue 2, 2009, Pages 128-135

Novel variants of the human flavin-containing monooxygenase 3 (FMO3) gene associated with trimethylaminuria

Author keywords

Flavin containing monooxygenase; FMO3; K415 frame shift; Novel mutations; Novel variants; TMAu; Trimethylaminuria; V187A

Indexed keywords

AMINO ACID; DIMETHYLANILINE MONOOXYGENASE; DIMETHYLANILINE MONOOXYGENASE 3; TRIMETHYLAMINE; TRIMETHYLAMINE OXIDE; UNCLASSIFIED DRUG;

EID: 67349179951     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2009.02.006     Document Type: Article
Times cited : (31)

References (42)
  • 2
    • 0036076899 scopus 로고    scopus 로고
    • Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase
    • Hines R.N., Hopp K.A., Franco J., Saeian K., and Begun F.P. Alternative processing of the human FMO6 gene renders transcripts incapable of encoding a functional flavin-containing monooxygenase. Mol. Pharmacol. 62 (2002) 320-325
    • (2002) Mol. Pharmacol. , vol.62 , pp. 320-325
    • Hines, R.N.1    Hopp, K.A.2    Franco, J.3    Saeian, K.4    Begun, F.P.5
  • 3
    • 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 I.R., and Shephard E.A. Organization and evolution of the flavin-containing monooxygenase genes of human and mouse: identification of novel gene and pseudogene clusters. Pharmacogenetics 14 (2004) 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
  • 5
    • 0036786378 scopus 로고    scopus 로고
    • Interindividual differences of human flavin-containing monooxygenase 3: genetic polymorphisms and functional variation
    • Cashman J.R., and Zhang J. Interindividual differences of human flavin-containing monooxygenase 3: genetic polymorphisms and functional variation. Drug Metab. Dispos. 30 (2002) 1043-1052
    • (2002) Drug Metab. Dispos. , vol.30 , pp. 1043-1052
    • Cashman, J.R.1    Zhang, J.2
  • 7
    • 0033582091 scopus 로고    scopus 로고
    • Trimethylaminuria: susceptibility of heterozygotes
    • Mitchell S.C. Trimethylaminuria: susceptibility of heterozygotes. Lancet 354 (1999) 2164-2165
    • (1999) Lancet , vol.354 , pp. 2164-2165
    • Mitchell, S.C.1
  • 8
    • 0035061010 scopus 로고    scopus 로고
    • Trimethylaminuria: the fish malodor syndrome
    • Mitchell S.C., and Smith R.L. Trimethylaminuria: the fish malodor syndrome. Drug Metab. Dispos. 29 (2001) 517-521
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 517-521
    • Mitchell, S.C.1    Smith, R.L.2
  • 9
    • 0030472235 scopus 로고    scopus 로고
    • Exacerbation of symptoms of fish-odour syndrome during menstruation
    • Zhang A.Q., Mitchell S.C., and Smith R.L. Exacerbation of symptoms of fish-odour syndrome during menstruation. Lancet 348 (1996) 1740-1741
    • (1996) Lancet , vol.348 , pp. 1740-1741
    • Zhang, A.Q.1    Mitchell, S.C.2    Smith, R.L.3
  • 10
    • 1642390782 scopus 로고    scopus 로고
    • Effects of the dietary supplements, activated charcoal and copper chlorophyllin, on urinary excretion of trimethylamine in Japanese trimethylaminuria patients
    • Yamazaki H., Fujieda M., Togashi M., Saito T., Preti G., Cashman J.R., and Kamataki T. Effects of the dietary supplements, activated charcoal and copper chlorophyllin, on urinary excretion of trimethylamine in Japanese trimethylaminuria patients. Life Sci. 74 (2004) 2739-2747
    • (2004) Life Sci. , vol.74 , pp. 2739-2747
    • Yamazaki, H.1    Fujieda, M.2    Togashi, M.3    Saito, T.4    Preti, G.5    Cashman, J.R.6    Kamataki, T.7
  • 11
    • 33847342912 scopus 로고    scopus 로고
    • Effect of genetic variants of the human flavin-containing monooxygenase 3 on N- and S-oxygenation activities
    • Shimizu M., Yano H., Nagashima S., Murayama N., Zhang J., Cashman J.R., and Yamazaki H. Effect of genetic variants of the human flavin-containing monooxygenase 3 on N- and S-oxygenation activities. Drug Metab. Dispos. 35 (2007) 328-330
    • (2007) Drug Metab. Dispos. , vol.35 , pp. 328-330
    • Shimizu, M.1    Yano, H.2    Nagashima, S.3    Murayama, N.4    Zhang, J.5    Cashman, J.R.6    Yamazaki, H.7
  • 12
    • 33846978122 scopus 로고    scopus 로고
    • Transient trimethylaminuria related to menstruation
    • Shimizu M., Cashman J.R., and Yamazaki H. Transient trimethylaminuria related to menstruation. BMC Med. Genet. 8 (2007) 2
    • (2007) BMC Med. Genet. , vol.8 , pp. 2
    • Shimizu, M.1    Cashman, J.R.2    Yamazaki, H.3
  • 16
    • 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 J.R. 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 (1993) 425-429
    • (1993) Chem. Res. Toxicol. , vol.6 , pp. 425-429
    • Lomri, N.1    Yang, Z.2    Cashman, J.R.3
  • 17
    • 0025151081 scopus 로고
    • Substrate specificities of rabbit lung and porcine liver flavin-containing monooxygenases: differences due to substrate size
    • Nagata T., Williams D.E., and Ziegler D.M. Substrate specificities of rabbit lung and porcine liver flavin-containing monooxygenases: differences due to substrate size. Chem. Res. Toxicol. 3 (1990) 372-376
    • (1990) Chem. Res. Toxicol. , vol.3 , pp. 372-376
    • Nagata, T.1    Williams, D.E.2    Ziegler, D.M.3
  • 19
    • 0042383168 scopus 로고    scopus 로고
    • Deleterious mutations in the flavin-containing monooxygenase 3 (FMO3) gene causing trimethylaminuria
    • Zhang J., Tran Q., Lattard V., and Cashman J.R. Deleterious mutations in the flavin-containing monooxygenase 3 (FMO3) gene causing trimethylaminuria. Pharmacogenetics 13 (2003) 495-500
    • (2003) Pharmacogenetics , vol.13 , pp. 495-500
    • Zhang, J.1    Tran, Q.2    Lattard, V.3    Cashman, J.R.4
  • 20
    • 0035201442 scopus 로고    scopus 로고
    • Population distribution of human flavin-containing monooxygenase form 3: gene polymorphisms
    • Cashman J.R., Zhang J., Leushner J., and Braun A. Population distribution of human flavin-containing monooxygenase form 3: gene polymorphisms. Drug Metab. Dispos. 29 (2001) 1629-1637
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 1629-1637
    • Cashman, J.R.1    Zhang, J.2    Leushner, J.3    Braun, A.4
  • 21
    • 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 Y.A., Lin J., Russell B., Luy L., Berkman C., and Cashman J. Characterization of two human flavin-containing monooxygenase (form 3) enzymes expressed in Escherichia coli as maltose binding protein fusions. Drug Metab. Dispos. 25 (1997) 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
  • 22
    • 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 J.R. Two new polymorphisms of the FMO3 gene in Caucasian and African-American populations: comparative genetic and functional studies. Drug Metab. Dispos. 31 (2003) 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
  • 23
    • 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 M.A., Haehner-Daniels B.D., Wrighton S.A., Rettie A.E., and Hall S.D. Stereoselective sulfoxidation of sulindac sulfide by flavin-containing monooxygenases. Comparison of human liver and kidney microsomes and mammalian enzymes. Biochem. Pharmacol. 60 (2000) 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
  • 24
    • 29144492916 scopus 로고    scopus 로고
    • Polymorphisms of the Flavin containing monooxygenase 3 (FMO3) gene do not predispose to essential hypertension in Caucasians
    • Dolan C., Shields D.C., Stanton A., O'Brien E., Lambert D.M., O'Brien J.K., and Treacy E.P. Polymorphisms of the Flavin containing monooxygenase 3 (FMO3) gene do not predispose to essential hypertension in Caucasians. BMC Med. Genet. 6 (2005) 41
    • (2005) BMC Med. Genet. , vol.6 , pp. 41
    • Dolan, C.1    Shields, D.C.2    Stanton, A.3    O'Brien, E.4    Lambert, D.M.5    O'Brien, J.K.6    Treacy, E.P.7
  • 26
    • 0036265797 scopus 로고    scopus 로고
    • Human flavin-containing monooxygenase (form 3): polymorphisms and variations in chemical metabolism
    • Cashman J.R. Human flavin-containing monooxygenase (form 3): polymorphisms and variations in chemical metabolism. Pharmacogenomics 3 (2002) 325-339
    • (2002) Pharmacogenomics , vol.3 , pp. 325-339
    • Cashman, J.R.1
  • 27
    • 0030667523 scopus 로고    scopus 로고
    • Missense mutation in flavin-containing mono-oxygenase 3 gene, FMO3, underlies fish-odour syndrome
    • Dolphin C.T., Janmohamed A., Smith R.L., Shephard E.A., and Phillips I.R. Missense mutation in flavin-containing mono-oxygenase 3 gene, FMO3, underlies fish-odour syndrome. Nat. Genet. 17 (1997) 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
  • 28
    • 34547668504 scopus 로고    scopus 로고
    • Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria
    • Yeung C.K., Adman E.T., and Rettie A.E. Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria. Arch. Biochem. Biophys. 464 (2007) 251-259
    • (2007) Arch. Biochem. Biophys. , vol.464 , pp. 251-259
    • Yeung, C.K.1    Adman, E.T.2    Rettie, A.E.3
  • 29
    • 33751535481 scopus 로고    scopus 로고
    • Investigation of structure and function of a catalytically efficient variant of the human flavin-containing monooxygenase form 3
    • Borbas T., Zhang J., Cerny M.A., Liko I., and Cashman J.R. Investigation of structure and function of a catalytically efficient variant of the human flavin-containing monooxygenase form 3. Drug Metab. Dispos. 34 (2006) 1995-2002
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 1995-2002
    • Borbas, T.1    Zhang, J.2    Cerny, M.A.3    Liko, I.4    Cashman, J.R.5
  • 31
    • 44349089600 scopus 로고    scopus 로고
    • Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase
    • Alfieri A., Malito E., Orru R., Fraaije M.W., and Mattevi A. Revealing the moonlighting role of NADP in the structure of a flavin-containing monooxygenase. Proc. Natl. Acad. Sci. USA 105 (2008) 6572-6577
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 6572-6577
    • Alfieri, A.1    Malito, E.2    Orru, R.3    Fraaije, M.W.4    Mattevi, A.5
  • 33
    • 0019876857 scopus 로고
    • The oxidative half-reaction of liver microsomal FAD-containing monooxygenase
    • Beaty N.B., and Ballou D.P. The oxidative half-reaction of liver microsomal FAD-containing monooxygenase. J. Biol. Chem. 256 (1981) 4619-4625
    • (1981) J. Biol. Chem. , vol.256 , pp. 4619-4625
    • Beaty, N.B.1    Ballou, D.P.2
  • 34
    • 0019876857 scopus 로고
    • The reductive half-reaction of liver microsomal FAD-containing monooxygenase
    • Beaty N.B., and Ballou D.P. The reductive half-reaction of liver microsomal FAD-containing monooxygenase. J. Biol. Chem. 256 (1981) 4611-4618
    • (1981) J. Biol. Chem. , vol.256 , pp. 4611-4618
    • Beaty, N.B.1    Ballou, D.P.2
  • 35
    • 0022980412 scopus 로고
    • Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates
    • Jones K.C., and Ballou D.P. Reactions of the 4a-hydroperoxide of liver microsomal flavin-containing monooxygenase with nucleophilic and electrophilic substrates. J. Biol. Chem. 261 (1986) 2553-2559
    • (1986) J. Biol. Chem. , vol.261 , pp. 2553-2559
    • Jones, K.C.1    Ballou, D.P.2
  • 36
    • 0018801101 scopus 로고
    • The liver microsomal FAD-containing monooxygenase. Spectral characterization and kinetic studies
    • Poulsen L.L., and Ziegler D.M. The liver microsomal FAD-containing monooxygenase. Spectral characterization and kinetic studies. J. Biol. Chem. 254 (1979) 6449-6455
    • (1979) J. Biol. Chem. , vol.254 , pp. 6449-6455
    • Poulsen, L.L.1    Ziegler, D.M.2
  • 37
    • 0023894686 scopus 로고
    • Flavin-containing monooxygenases: catalytic mechanism and substrate specificities
    • Ziegler D.M. Flavin-containing monooxygenases: catalytic mechanism and substrate specificities. Drug Metab. Rev. 19 (1988) 1-32
    • (1988) Drug Metab. Rev. , vol.19 , pp. 1-32
    • Ziegler, D.M.1
  • 38
    • 33845210972 scopus 로고    scopus 로고
    • Stop codon mutations in the flavin-containing monooxygenase 3 (FMO3) gene responsible for trimethylaminuria in a Japanese population
    • Yamazaki H., Fujita H., Gunji T., Zhang J., Kamataki T., Cashman J.R., and Shimizu M. Stop codon mutations in the flavin-containing monooxygenase 3 (FMO3) gene responsible for trimethylaminuria in a Japanese population. Mol. Genet. Metab. 90 (2007) 58-63
    • (2007) Mol. Genet. Metab. , vol.90 , pp. 58-63
    • Yamazaki, H.1    Fujita, H.2    Gunji, T.3    Zhang, J.4    Kamataki, T.5    Cashman, J.R.6    Shimizu, M.7
  • 40
    • 0015337668 scopus 로고
    • Microsomal oxidase. IV. Properties of a mixed-function amine oxidase isolated from pig liver microsomes
    • Ziegler D.M., and Mitchell C.H. Microsomal oxidase. IV. Properties of a mixed-function amine oxidase isolated from pig liver microsomes. Arch. Biochem. Biophys. 150 (1972) 116-125
    • (1972) Arch. Biochem. Biophys. , vol.150 , pp. 116-125
    • Ziegler, D.M.1    Mitchell, C.H.2
  • 41
    • 0033959521 scopus 로고    scopus 로고
    • Population-specific polymorphisms of the human FMO3 gene: significance for detoxication
    • Cashman J.R., Akerman B.R., Forrest S.M., and Treacy E.P. Population-specific polymorphisms of the human FMO3 gene: significance for detoxication. Drug Metab. Dispos. 28 (2000) 169-173
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 169-173
    • Cashman, J.R.1    Akerman, B.R.2    Forrest, S.M.3    Treacy, E.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.