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Can our knowledge of monoamine oxidase (MAO) help in the design of better MAO inhibitors?

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Amine Oxidases: Function and Dysfunction

Part of the book series: Journal of Neural Transmission ((NEURAL SUPPL,volume 41))

Summary

This paper presents a rapid overview of the mechanism by which monoamine oxidase (MAO) catalyzes the deamination of its substrates, and highlights the stereoselective nature of the active site of the enzyme. With the help of a few selected examples it is also discussed which structural factors are thought to have a preponderant influence on the affinity and selectivity of molecules towards the active site of either form of MAO.

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Author information

Authors and Affiliations

  1. Famitalia Carlo Erba-Research and Development, Via C. Imbonati 24, I-20159, Milan, Italy

    Dr. P. Dostert

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  1. Dr. P. Dostert
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Editor information

Editors and Affiliations

  1. Biochemistry Department, Trinity College, Dublin, Ireland

    K. F. Tipton

  2. Department of Pharmacology, Technion, Haifa, Israel

    M. B. H. Youdim

  3. School of Pharmacy and Biomedicai Sciences, University of Portsmouth, UK

    C. J. Barwell

  4. Department of Pharmacology, University of Cambridge, UK

    B. A. Callingham

  5. Department of Pharmacology and Clinical Pharmacology, University of Dundee, UK

    G. A. Lyles

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© 1994 Springer-Verlag

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Dostert, P. (1994). Can our knowledge of monoamine oxidase (MAO) help in the design of better MAO inhibitors?. In: Tipton, K.F., Youdim, M.B.H., Barwell, C.J., Callingham, B.A., Lyles, G.A. (eds) Amine Oxidases: Function and Dysfunction. Journal of Neural Transmission, vol 41. Springer, Vienna. https://doi.org/10.1007/978-3-7091-9324-2_35

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  • DOI: https://doi.org/10.1007/978-3-7091-9324-2_35

  • Publisher Name: Springer, Vienna

  • Print ISBN: 978-3-211-82521-1

  • Online ISBN: 978-3-7091-9324-2

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