Abstract
The flavin-containing monooxygenase (EC 1.14.13.8) (FMO), originally described as an amine oxidase, was subsequently shown to be a versatile sulfur oxidase, the early studies being summarized by Ziegler (1). The FMO has been shown more recently to be a phosphorus oxidase (2,3). This enzyme and the cytochrome P450-dependent monooxygenase system are the two principal enzymes that catalyze the oxidation of lipophilic xenobiotics to electrophilic products capable of further metabolism, either to readily excretable conjugation products or to reactive intermediates with potential for adverse effects. Much of what is known about the substrate specificity of the FMO, is summarized in a recent review (4). Purification of pig liver FMO was accomplished some time ago (5) and the ability of the solubilized enzyme to catalyze the oxidation of the same wide variety of nucleophilic nitrogen, sulfur and phosphorus compounds as the membrane-bound enzyme has been established (1-5). The physiological role for this enzyme is not well known but may be involved in the maintenance of cellular thiol:disulfide ratios by the oxidation of cysteamine to cystamine (6).
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© 1991 Plenum Press, New York
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Hodgson, E., Levi, P.E. (1991). The Flavin-Containing Monooxygenase (EC 1.14.13.8). In: Arinç, E., Schenkman, J.B., Hodgson, E. (eds) Molecular Aspects of Monooxygenases and Bioactivation of Toxic Compounds. NATO ASI Series Advanced Science Institutes Series, vol 202. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-7284-4_2
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DOI: https://doi.org/10.1007/978-1-4684-7284-4_2
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