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

Rona R. Ramsay

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

Rona R. Ramsay

Research output: Chapter in Book/Report/Conference proceeding › Chapter

13 Downloads (Pure)

Abstract

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 language	English
Title of host publication	Pharmaceutical Biocatalysis
Subtitle of host publication	Fundamentals, Enzyme Inhibitors, and Enzymes in Health and Diseases
Editors	Peter Grunwald
Place of Publication	Singapore
Publisher	Pan Stanford Publishing Pte. Ltd.
Chapter	10
Volume	4
ISBN (Print)	9789814800617
Publication status	Published - 31 Mar 2019

Publication series

Name	Series on Biocatalysis
Publisher	Pan Stanford Publishing Pte. Ltd., Singapore
Number	10
Volume	4

Keywords

Neurotransmitter metabolism
Inhibition
Kinetics
Chemical mechanism
Monoamine oxidase
Computational tools

Access to Document

Ramsay-2019-PharmBiocatalysis-AAM
© 2019, Pan Stanford Publishing Ptd Ltd. This work is made available online by kind permission of the publisher. This is the author created, accepted version manuscript following peer review and may differ slightly from the final published version.
Accepted author manuscript, 1.31 MB

Cite this

@inbook{4640c0cb0dcc452e83ab44e44f21201f,

title = "Molecular aspects of the activity and inhibition of the FAD-containing monoamine oxidases",

abstract = "1. Introduction2. FAD: the catalytic cofactor2.1 FAD is covalently attached to MAO 2.3 FAD is modified by irreversible inhibitors3. MAO proteins3.1 MAO protein expression and turnover3.2 MAO A and MAO B structures and active sites3.3 MAO chemical mechanism3.4 MAO kinetic mechanism: two-substrate kinetics4. Substrate Specificity of these Promiscuous Enzymes4.1 Neurotransmitter metabolism4.2 Metabolism of biogenic amines4.3 Products from MAO catalysis5. Inhibition of MAO5.1 Reversible inhibitors of MAO5.2 Examples of tight binding reversible inhibitors of MAO5.3 Examples of irreversible inhibitors of MAO6. Computational innovation6.1 Theoretical elucidation of mechanism6.2 Data-mining and tools for drug discovery7. Conclusion: the future for MAO inhibition in multi-target drugs",

keywords = "Neurotransmitter metabolism, Inhibition, Kinetics, Chemical mechanism, Monoamine oxidase, Computational tools",

author = "Ramsay, {Rona R.}",

year = "2019",

month = mar,

day = "31",

language = "English",

isbn = "9789814800617 ",

volume = "4",

series = "Series on Biocatalysis",

publisher = "Pan Stanford Publishing Pte. Ltd.",

number = "10",

editor = "Peter Grunwald",

booktitle = "Pharmaceutical Biocatalysis",

}

Molecular aspects of the activity and inhibition of the FAD-containing monoamine oxidases. / Ramsay, Rona R.
Pharmaceutical Biocatalysis: Fundamentals, Enzyme Inhibitors, and Enzymes in Health and Diseases . ed. / Peter Grunwald. Vol. 4 Singapore: Pan Stanford Publishing Pte. Ltd., 2019. (Series on Biocatalysis; Vol. 4, No. 10).

Research output: Chapter in Book/Report/Conference proceeding › Chapter

TY - CHAP

T1 - Molecular aspects of the activity and inhibition of the FAD-containing monoamine oxidases

AU - Ramsay, Rona R.

PY - 2019/3/31

Y1 - 2019/3/31

N2 - 1. Introduction2. FAD: the catalytic cofactor2.1 FAD is covalently attached to MAO 2.3 FAD is modified by irreversible inhibitors3. MAO proteins3.1 MAO protein expression and turnover3.2 MAO A and MAO B structures and active sites3.3 MAO chemical mechanism3.4 MAO kinetic mechanism: two-substrate kinetics4. Substrate Specificity of these Promiscuous Enzymes4.1 Neurotransmitter metabolism4.2 Metabolism of biogenic amines4.3 Products from MAO catalysis5. Inhibition of MAO5.1 Reversible inhibitors of MAO5.2 Examples of tight binding reversible inhibitors of MAO5.3 Examples of irreversible inhibitors of MAO6. Computational innovation6.1 Theoretical elucidation of mechanism6.2 Data-mining and tools for drug discovery7. Conclusion: the future for MAO inhibition in multi-target drugs

AB - 1. Introduction2. FAD: the catalytic cofactor2.1 FAD is covalently attached to MAO 2.3 FAD is modified by irreversible inhibitors3. MAO proteins3.1 MAO protein expression and turnover3.2 MAO A and MAO B structures and active sites3.3 MAO chemical mechanism3.4 MAO kinetic mechanism: two-substrate kinetics4. Substrate Specificity of these Promiscuous Enzymes4.1 Neurotransmitter metabolism4.2 Metabolism of biogenic amines4.3 Products from MAO catalysis5. Inhibition of MAO5.1 Reversible inhibitors of MAO5.2 Examples of tight binding reversible inhibitors of MAO5.3 Examples of irreversible inhibitors of MAO6. Computational innovation6.1 Theoretical elucidation of mechanism6.2 Data-mining and tools for drug discovery7. Conclusion: the future for MAO inhibition in multi-target drugs

KW - Neurotransmitter metabolism

KW - Inhibition

KW - Kinetics

KW - Chemical mechanism

KW - Monoamine oxidase

KW - Computational tools

UR - http://www.panstanford.com/books/9789814800617.html#

M3 - Chapter

SN - 9789814800617

VL - 4

T3 - Series on Biocatalysis

BT - Pharmaceutical Biocatalysis

A2 - Grunwald, Peter

PB - Pan Stanford Publishing Pte. Ltd.

CY - Singapore

ER -

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

Abstract

Publication series

Keywords

Access to Document

Other files and links

Fingerprint

Cite this