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Mechanism, multiple forms and substrate specificities of flavin-containing mono-oxygenases

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N-Oxidation of Drugs

Abstract

Enzymes bearing flavin prosthetic groups are quite common in all eukaryotic and prokaryotic organisms. The tricyclic ring of isoalloxizine is an exceptionally versatile molecule that in different microenvironments carries out a variety of different biological redox functions. Most of these are well known and the present discussion will be restricted to a subgroup of flavin-dependent mono-oxygenases that catalyse the oxidation of an exceptionally broad range of substrates via a mechanism distinctly different from all other mono-oxygenases or oxidases.

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Authors and Affiliations

  1. Clayton Foundation Biochemical Institute and Department of Chemistry, The University of Texas at Austin, 78712, Austin, TX, USA

    D. M. Ziegler

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  1. D. M. Ziegler
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Editors and Affiliations

  1. Ludwig-Maximilians-Universität München, Munich, Germany

    P. Hlavica (Full Professor of Pharmacology and Toxicology) (Full Professor of Pharmacology and Toxicology)

  2. Chelsea Department of Pharmacy, King’s College, University of London, UK

    L. A. Damani (Lecturer in Biopharmacy) (Lecturer in Biopharmacy)

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© 1991 Springer Science+Business Media Dordrecht

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Ziegler, D.M. (1991). Mechanism, multiple forms and substrate specificities of flavin-containing mono-oxygenases. In: Hlavica, P., Damani, L.A. (eds) N-Oxidation of Drugs. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-3112-4_4

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  • DOI: https://doi.org/10.1007/978-94-011-3112-4_4

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-94-010-5378-5

  • Online ISBN: 978-94-011-3112-4

  • eBook Packages: Springer Book Archive

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