GENETIC POLYMORPHISMS OF FLAVIN-CONTAINING MONOOXYGENASE (FMO)

REFERENCES

• Ziegler D.M. Recent Studies on the Structure and Function of Multisubstrate Flavin-Containing Monooxygenases. Annu. Rev. Pharmacol. Toxicol. 1993; 33: 179–199
   PubMed Web of Science ®Google Scholar
• Cashman J.R. Structural and Catalytic Properties of the Mammalian Flavin-Containing Monooxygenase. Chem. Res. Toxicol. 1995; 8(2)165–181
   Web of Science ®Google Scholar
• Ziegler D.M. Metabolic Oxygenation of Organic Nitrogen and Sulfur Compounds. Drug Metabolism and Drug Toxicity, J.R. Mitchell, M.G. Horning. Raven Press, New York 1984; 33–53
   Google Scholar
• Ziegler D.M., Mitchell C.H. Microsomal Oxidase IV: Properties of Mixed-Function Amine Oxidase Isolated from Pig Liver Microsomes. Arch. Biochem. Biophys. 1972; 150(1)116–125
   PubMed Web of Science ®Google Scholar
• Williams D.E., Ziegler D.M., Nordin D.J., Hale S.E., Masters B.S.S. Rabbit Lung Flavin-Containing Monooxygenase Is Immunochemically and Catalytically Distinct from the Liver Enzyme. Biochem. Biophys. Res. Commun. 1984; 125(1)116–122
   PubMed Web of Science ®Google Scholar
• Tynes R.E., Sabourin P.J., Hodgson E. Identification of Distinct Hepatic and Pulmonary Forms of Microsomal Flavin-Containing Monooxygenase in the Mouse and Rabbit. Biochem. Biophys. Res. Commun. 1985; 126(3)1069–1075
   PubMed Web of Science ®Google Scholar
• Hines R.N., Cashman J.R., Philpot R.M., Williams D.E., Ziegler D.M. The Mammalian Flavin-Containing Monooxygenases: Molecular Characterization and Regulation of Expression. Toxicol. Appl. Pharmacol. 1994; 125(1)1–6
   PubMed Web of Science ®Google Scholar
• Lawton M., Cashman J., Cresteil T., Dolphin C., Elfarra A., Hines R.N., Hodgson E., Kimura T., Ozols J., Phillips I., Philpot R., Poulsen L., Rettie S., Williams D., Ziegler D. A Nomenclature for the Mammalian Flavin-Containing Monooxygenase Gene Family Based on Amino Acid Sequence Identities. Arch. Biochem. Biophys. 1994; 308(1)254–257
   PubMed Web of Science ®Google Scholar
• Williams D.E. Factors Regulating the Activity of the Rabbit Lung Flavin-Containing Monooxygenase. N-Oxidation of Drugs. Biochemistry, Pharmacology, Toxicology, P. Hlavica, L.A. Damani. Chapman and Hall, New York 1991; 91–105
   Google Scholar
• Mitchell S.C., Smith R.L. Trimethylaminuria: The Fish Malodor Syndrome. Drug Metab. Dispos. 2001; 29(4 pt 2)517–521
   PubMed Web of Science ®Google Scholar
• Cashman J.R., Bi Y.A., Lin J., Youil R., Knight M., Forrest S., Treacy E. Human Flavin-Containing Monooxygenase Form 3: cDNA Expression of the Enzymes Containing Amino Acid Substitutions Observed in Individuals with Trimethylaminuria. Chem. Res. Toxicol. 1997; 10(8)837–841
   PubMed Web of Science ®Google Scholar
• Dolphin C.T., Janmohamed A., Smith R.L., Shephard E.A., Phillips I.R. Missense Mutation in Flavin-Containing Monooxygenase 3 Gene, FMO3, Underlies Fish-Odour Syndrome. Nat. Genet. 1997; 17(4)491–494
   PubMed Web of Science ®Google Scholar
• Dolphin C.T., Riley J.H., Smith R.L., Shephard E.A., Phillips I.R. Structural Organization of the Human Flavin-Containing Monooxygenase 3 Gene (FMO3), the Favored Candidate for Fish-Odor Syndrome, Determined Directly from Genomic DNA. Genomics 1997; 46(2)260–267
   PubMed Web of Science ®Google Scholar
• Murphy H.C., Dolphin C.T., Janmohamed A., Holmes H.C., Michelakakis H., Shephard E.A., Chalmers R.A., Phillips I.R., Iles R.A. A Novel Mutation in the Flavin-Containing Monooxygenase 3 Gene, FMO3, that Causes Fish-Odour Syndrome: Activity of the Mutant Enzyme Assessed by Proton NMR Spectroscopy. Pharmacogenetics 2000; 10(5)439–451
   PubMedGoogle Scholar
• Basarab T., Ashton G.H., Menage H.P., McGrath J.A. Sequence Variations in the Flavin-Containing Monooxygenase 3 Gene (FMO3) in Fish Odour Syndrome. Br. J. Dermatol. 1999; 140(1)164–167
   PubMed Web of Science ®Google Scholar
• Treacy E.P., Akerman B.R., Chow L.M.L., Youil R., Bibeau C., Lin J., Bruce A.G., Knight M., Danks D.M., Cashman J.R., Forrest S.M. Mutations of the Flavin-Containing Monooxygenase Gene (FMO3) Cause Trimethylaminuria, a Defect in Detoxication. Hum. Mol. Genet. 1998; 7(5)839–845
   PubMed Web of Science ®Google Scholar
• Akerman B.R., Forrest S., Chow L., Youil R., Knight M., Treacy E.P. Two Novel Mutations of the FMO3 Gene in a Proband with Trimethylaminuria. Hum. Mutat. 1999; 13(5)376–379
   PubMed Web of Science ®Google Scholar
• Dolphin C.T., Janmohamed A., Smith R.L., Shephard E.A., Phillips I.R. Compound Heterozygosity for Missense Mutations in the Flavin-Containing Monooxygenase 3 (FMO3) Gene in Patients with Fish-Odour Syndrome. Pharmacogenetics 2000; 10(9)799–807
   PubMedGoogle Scholar
• Dolphin C.T., Beckett D.J., Janmohamed A., Cullingford T.E., Smith R.L., Shephard E.A., Phillips I.R. The Flavin-Containing Monooxygenase 2 Gene (FMO2) of Humans, But Not of Other Primates Encodes a Truncated, Nonfunctional Protein. J. Biol. Chem. 1998; 273(46)30599–30607
   PubMed Web of Science ®Google Scholar
• Lawton M.P., Gasser R., Tynes R.E., Hodgson E., Philpot R.M. The Flavin-Containing Monooxygenase Enzymes Expressed in Rabbit Liver and Lung Are Products of Related by Distinctly Different Genes. J. Biol. Chem. 1990; 265(10)5855–5861
   PubMed Web of Science ®Google Scholar
• Nikbakht K.N., Lawton M.P., Philpot R.M. Guinea Pig or Rabbit Lung Flavin-Containing Monooxygenases with Distinct Mobilities in SDS-PAGE Are Allelic Variants That Differ at Only Two Positions. Pharmacogenetics 1992; 2(5)207–216
   PubMedGoogle Scholar
• Yueh M.-F., Krueger S.K., Williams D.E. Pulmonary Flavin-Containing Monooxygenase (FMO) in Rhesus Macaque: Expression of FMO2 Protein, mRNA and Analysis of the cDNA. Biochim. Biophys. Acta 1997; 1350(3)267–271
   PubMed Web of Science ®Google Scholar
• Whetstine J.R., Yueh M.-F., McCarver D.G., Williams D.E., Park C.-S., Kang J.H., Cha Y.-N., Dolphin C.T., Shephard E.A., Phillips I.R., Hines R.N. Ethnic Differences in Human Flavin-Containing Monooxygenase 2 (FMO2) Polymorphisms: Detection of Expressed Protein in African-Americans. Toxicol. Appl. Pharmacol. 2000; 168(3)216–224
   PubMed Web of Science ®Google Scholar
• Raucy J.L., Schultz E.D., Wester M.R., Arora S., Johnston D.E., Omdahl J.L., Carpenter S.P. Human Chlorzoxazone Activity. Drug Metab. Dispos. 1997; 25(12)1429–1435
   PubMed Web of Science ®Google Scholar
• Raucy J.L., Schultz E.D., Kearins M.C., Arora S., Johnston D.E., Omdahl J.L., Eckmann L., Carpenter S.P. CYP2E1 Expression in Human Lymphocytes from Various Ethnic Populations. Alcohol. Clin. Exp. Res. 1999; 23(12)1868–1874
   PubMed Web of Science ®Google Scholar
• Cashman J.R., Akerman B.R., Forrest S.M., Treacy E.P. Population-Specific Polymorphisms of the Human FMO3 Gene: Significance for Detoxication. Drug Metab. Dispos. 2000; 28(2)169–173
   PubMed Web of Science ®Google Scholar
• Forrest S.M., Knight M., Akerman B.R., Cashman J.R., Treacy E.P. A Novel Deletion in Flavin-Containing Monooxygenase Gene (FMO3) in a Greek Patient with Trimethylaminuria. Pharmacogenetics 2001; 11(2)169–174
   PubMedGoogle Scholar
• Akerman B.R., Lemass H., Chow L.M., Lambert D.M., Greenberg C., Bibeau C., Mamer O.A., Treacy E.P. Trimethylaminuria Is Caused by Mutations of the FMO3 Gene in a North American Cohort. Mol. Genet. Metab. 1999; 68(1)24–31
   PubMed Web of Science ®Google Scholar
• Brunelle A., Bi Y.A., Lin J., Russel B., Luy L., Berkman C., Cashman J. Characterization of Two Human Flavin-Containing Monooxygenase (Form 3) Enzymes Expressed in Escherichia coli as Maltose Binding Protein Fusions. Drug Metab. Dispos. 1997; 25(8)1001–1007
   PubMed Web of Science ®Google Scholar
• Zschocke J., Kohmueller D., Quak E., Meissner T., Hoffmann G.F., Mayatepek E. Mild Trimethylaminuria Caused by Common Variants in FMO3 Gene. Lancet 1999; 354(9181)834–835
   PubMed Web of Science ®Google Scholar