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Research at St Andrews

Molecular aspects of the activity and inhibition of the FAD-containing monoamine oxidases

Research output: Chapter in Book/Report/Conference proceedingChapter


1. Introduction

2. FAD: the catalytic cofactor
2.1 FAD is covalently attached to MAO
2.3 FAD is modified by irreversible inhibitors

3. MAO proteins
3.1 MAO protein expression and turnover
3.2 MAO A and MAO B structures and active sites
3.3 MAO chemical mechanism
3.4 MAO kinetic mechanism: two-substrate kinetics

4. Substrate Specificity of these Promiscuous Enzymes
4.1 Neurotransmitter metabolism
4.2 Metabolism of biogenic amines
4.3 Products from MAO catalysis

5. Inhibition of MAO
5.1 Reversible inhibitors of MAO
5.2 Examples of tight binding reversible inhibitors of MAO
5.3 Examples of irreversible inhibitors of MAO

6. Computational innovation
6.1 Theoretical elucidation of mechanism
6.2 Data-mining and tools for drug discovery

7. Conclusion: the future for MAO inhibition in multi-target drugs


Original languageEnglish
Title of host publicationPharmaceutical Biocatalysis
Subtitle of host publicationFundamentals, Enzyme Inhibitors, and Enzymes in Health and Diseases
EditorsPeter Grunwald
Place of PublicationSingapore
Publisher Pan Stanford Publishing Pte. Ltd.
ISBN (Print)9789814800617
Publication statusPublished - 31 Mar 2019

Publication series

NameSeries on Biocatalysis
PublisherPan Stanford Publishing Pte. Ltd., Singapore

    Research areas

  • Neurotransmitter metabolism, Inhibition, Kinetics, Chemical mechanism, Monoamine oxidase, Computational tools

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ID: 258701840