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Flavin-Containing Monooxygenases: Substrate Specificity and Complex Metabolic Pathways

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Molecular Aspects of Oxidative Drug Metabolizing Enzymes

Part of the book series: NATO ASI Series ((ASIH,volume 90))

Abstract

The flavin-containing monooxygenase (EC 1.14.13.8)(FMO) is located in the endoplasmic reticulum of mammalian cells and is involved in the monooxygenation of a wide variety of xenobiotics. The FMO has a similar distribution and function to many of the isozymes of cytochrome P450 (P450). Originally described as an amine oxidase (Ziegler and Mitchell, 1972), it is now known to catalyze the oxidation of many organic, and some inorganic, chemicals (Ziegler, 1990, 1991). The FAD prosthetic group first reacts with NADPH and then molecular oxygen to give rise to the enzyme-bound hydroperoxyflavin responsible for the oxidation of suitable substrates. These initial reactions occur in the absence of substrate and the enzyme exists primarily in the hydroperoxyflavin form (Poulsen and Ziegler, 1979, Beaty and Ballou, 1981a,b). A consequence of this is that substrates, with few exceptions, have the same Vmax, although Km may vary.

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© 1995 Springer-Verlag Berlin Heidelberg

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Hodgson, E. et al. (1995). Flavin-Containing Monooxygenases: Substrate Specificity and Complex Metabolic Pathways. In: Arinç, E., Schenkman, J.B., Hodgson, E. (eds) Molecular Aspects of Oxidative Drug Metabolizing Enzymes. NATO ASI Series, vol 90. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-79528-2_12

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  • DOI: https://doi.org/10.1007/978-3-642-79528-2_12

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-79530-5

  • Online ISBN: 978-3-642-79528-2

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