HUMAN AND PLANT FLAVIN-CONTAINING MONOOXYGENASE N-OXYGENATION OF AMINES: DETOXICATION VS. BIOACTIVATION

REFERENCES

• Ziegler D.M. Microsomal Flavin-Containing Monooxygenase: Oxygenation of Nucleophilic Nitrogen and Sulfur Compounds. Enzymatic Basis of Detoxication, W.B. Jakoby. Academic Press, New York 1980; Vol. 1: 201–277
   Google Scholar
• Cashman J.R. Structural and Catalytic Properties of the Mammalian Flavin-Containing Monooxygenase. Chem. Res. Toxicol. 1995; 8: 165–181
   Web of Science ®Google Scholar
• Hajjar N., Hodgson E. Mammalian Hepatic Microsomal FAD-Containing Monooxygenase: Evidence for It's Role in the Sulfoxidation of Pesticides. Science 1980; 209: 1134–1136
   PubMed Web of Science ®Google Scholar
• Ziegler D.M. Flavin-Containing Monooxygenase: Catalytic Mechanism and Substrate Specificities. Drug Metab. Rev. 1988; 19: 1–31
   PubMed Web of Science ®Google Scholar
• Ziegler D.M. Flavin-Containing Monooxygenases: Enzymes Adapted for Multisubstrate Specificity. Trends Pharmacol. Sci. 1990; 11: 321–324
   PubMed Web of Science ®Google Scholar
• Lawton M.P., Cashman J.R., Cresteil T., Dolphin C., Elfarra A., Hines R.N., Hodgson E., Kimura T., Ozols J., Phillips I., Philpot R.M., Poulsen L.L., Rettie A.E., Williams D.E., Ziegler D.M. A Nomenclature for the Mammalian Flavin-Containing Monooxygenase Gene Family Based on Amino Acid Sequence Identities. Arch. Biochem. Biophys. 1994; 308: 254–257
   PubMed Web of Science ®Google Scholar
• Ryerson C.C., Ballou D.P., Walsh C. Mechanistic Studies on Cyclohexanone Oxygenase. Biochemistry 1982; 21: 2644–2655
   PubMed Web of Science ®Google Scholar
• Suh J.K., Poulsen L.L., Ziegler D.M., Tobertus J.D. Molecular Cloning and Kinetic Characterization of a Flavin-Containing Monooxygenase from Saccharomyces cerevisiae. Arch. Biochem. Biophys. 1996; 336: 268–274
   PubMed Web of Science ®Google Scholar
• Zhao Y., Christensen S.K., Frankhauser C., Cashman J.R., Cohen J.D., Weigel D., Chory J. A Role for Flavin-Monooxygenase-like Enzymes in Auxin Biosynthesis. Science 2001; 291: 306–309
   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: 1–6
   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: 260–267
   PubMed Web of Science ®Google Scholar
• Wyatt M.K., Overby L.H., Lawton M.P., Philpot R.M. Identification of Amino Acid Residues Associated with Modulation of Flavin-Containing Monooxygenase (FMO) Activity of Imipramine: Structure/Function Studies in Pig and Rabbit. Biochemistry 1998; 37: 5930–5938
   PubMed Web of Science ®Google Scholar
• Treacy E.P., Akerman B., Chow L.M.L., Youil R., Bibeau C., Lin J., Bruce 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: 839–845
   PubMed Web of Science ®Google Scholar
• Gasser R., Tynes R.E., Lawton M.P., Korsmeyer K.K., Ziegler D.M., Philpot R.M. The Flavin-Containing Monooxygenase Expressed in Pig Liver: Primary Sequence, Distribution, and Evidence for a Single Gene. Biochemistry 1990; 29: 119–124
   PubMed Web of Science ®Google Scholar
• Lomri N., Quimin G., Cashman J.R. Molecular Cloning of the Human Liver Flavin-Containing Monooxygenase Form II cDNA Structure and Expression. Proc. Natl Acad. Sci. USA 1992; 89: 1685–1689
   PubMed Web of Science ®Google Scholar
• Lawton M.P., Philpot R.M. 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. 1993; 268: 5728–5734
   PubMed Web of Science ®Google Scholar
• Korsmeyer K.K., Guan S., Yang Z.C., Falick A.M., Ziegler D.M., Cashman J.R. N-Glycosylation of Pig Flavin-Containing Monooxygenase Form 1: Determination of Protein Modification by Mass Spectrometry. Chem. Res. Toxicol. 1998; 11: 1145–1153
   PubMed Web of Science ®Google Scholar
• Brunnelle A., Bi Y.A., Lin J., Russell B., Luy L., Berkman C., Cashman J.R. Characterization of Two Human Flavin-Containing Monooxygenase (Form 3) Enzymes Expressed in Escherichia coli as Maltose Binding Protein Fusions. Drug Metab. Dispos. 1997; 25: 1001–1007
   PubMed Web of Science ®Google Scholar
• Ziegler D.M., Poulsen L.L. Catalytic Mechanism of FMO-Catalyzed N- and S-Oxidations. Drug Metabolism: Towards the Next Millenium, N. Gooderham. IOS Press, London 1998; 30–38
   Google Scholar
• Christensen D. What's That Smell?. Sci. News 1999; 155: 316–317
   Google Scholar
• Cashman J.R. Flavin Monooxygenase. Handbook of Enzyme Systems That Metabolize Drugs and Other Xenobiotics, C. Ioannodes. John Wiley & Sons, West SussexUK 2001; 67–93
   Google Scholar
• Poulsen L.L., Ziegler D.M. The Liver Microsomal FAD-Containing Monooxygenases. Spectral Characterization and Kinetic Studies. J. Biol. Chem. 1979; 254: 6449–6455
   PubMed Web of Science ®Google Scholar
• Beaty N.B., Ballou D.P. The Oxidative Half-Reaction of Liver Microsomal FAD-Containing Monooxygenase. J. Biol. Chem. 1981; 256: 4619–4625
   PubMed Web of Science ®Google Scholar
• Beaty N.B., Ballou D.P. The Reductive Half-Reaction of Liver Microsomal FAD-Containing Monooxygenase. J. Biol. Chem. 1981; 256: 4611–4618
   PubMed Web of Science ®Google Scholar
• Ball S.S., Bruice T.C. Oxidation of Amines by a 4a-Hydroperoxyflavin. J. Am. Chem. Soc. 1983; 102: 6498–6503
   Google Scholar
• 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. Stereoselectivity in S- and N-Oxygenation by the Mammalian Flavin-Containing Monooxygenase and Cytochrome P-450 Monooxygenases. Drug Metab. Rev. 1998; 30: 675–708
   PubMed Web of Science ®Google Scholar
• Kim Y.M., Ziegler D.M. Size Limits of Thiocarbamides Accepted as Substrates by Human Flavin-Containing Monooxygenase 1. Drug Metab. Dispos. 2000; 28: 1003–1006
   PubMed Web of Science ®Google Scholar
• Cashman J.R., Park S.B., Berkman C.E., Cashman L.E. Role of Hepatic Flavin-Containing Monooxygenase 3 in Drug and Chemical Metabolism in Adult Humans. Chem. Biol. Interact. 1995; 96: 33–46
   PubMed Web of Science ®Google Scholar
• Cashman J.R. Human Flavin-Containing Monooxygenase: Substrate Specificity and Role in Drug Metabolism. Curr. Drug Metab. 2000; 1: 181–191
   PubMed Web of Science ®Google Scholar
• Weigel D., Ahn J.H., Blázquez M.A., Borevitz J.O., Christensen S.K., Fankhauser C., Ferrándiz C., Kardailsky I., Malancharuvil E.J., Neff M.M., Nguyen J.T., Sato S., Wang Z.Y., Xia Y., Dixon R.A., Harrison M.J., Lamb C.J., Yanofsky M.F., Chory J. Activation Tagging in Arabidopsis. Plant Physiol. 2000; 122: 1003–1014
   PubMed Web of Science ®Google Scholar
• Lin J., Cashman J.R. Detoxication of Tyramine by the Flavin-Containing Monooxygenase: Stereoselective Formation of the trans-Oxime. Chem. Res. Toxicol. 1997; 10: 842–852
   PubMed Web of Science ®Google Scholar
• Lin J., Cashman J.R. N-Oxygenation of Phenethylamine to the trans-Oxime by Adult Human Liver Flavin-Containing Monooxygenase and Retroreduction of Phenethylamine Hydroxylamine by Human Liver Microsomes. J. Pharmacol. Exp. Ther. 1997; 282: 1269–1279
   PubMed Web of Science ®Google Scholar
• Poulsen L.L., Taylor K.K., Williams D.E., Masters B.S.S., Ziegler D.M. Substrate Specificity of the Rabbit Lung Flavin-Containing Monooxygenase for Amines. Oxidation Products of Primary Alkylamines. Mol. Pharmacol. 1986; 30: 680–685
   PubMed Web of Science ®Google Scholar