INSIDE THE PLASMA AMINE OXIDASE : PRELIMINARY DRUG DISCOVERY STUDY OF PLASMA AMINE OXIDASE: STRUCTURAL BASIS OF SUBSTRATE AND INHIBITORY ACTIVITY OF BOVINE PLASMA AMINE OXIDASE

Language: English

Published by VDM Verlag Dr. Müller, 2010

3639255682 / 9783639255683

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nach der Bestellung gedruckt Neuware - Printed after ordering - The copper-containing amine oxidases, like bovine plasma amine oxidase (BPAO), carry out a transaminative oxidation of primary amines to aldehydes via use of an active site Tyr-derived 2,4,5-trihydroxyphenylalanine quinone (TPQ) cofactor. Propargylamine is a potent inactivator of BPAO (IC50 = 3 µM), possibly through active-site modification by the a,ß-unsaturated aldehyde turnover product, but the simple structure is expected to confer low selectivity. On the basis of the finding by previous students that certain extended conjugation analogs such as 1,6-diamino-2,4- hexadiyne and 3-cyanopropargylamine preserve strong inactivation potency, other extended conjugation analogs of propargylamine were evaluated. In particular, 1-amino-2,4-hexadiynes with a 6-OH rather than 6-NH2 group were found to be potent inhibitors.

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Title
INSIDE THE PLASMA AMINE OXIDASE : PRELIMINARY DRUG DISCOVERY STUDY OF PLASMA AMINE OXIDASE: STRUCTURAL BASIS OF SUBSTRATE AND INHIBITORY ACTIVITY OF BOVINE PLASMA AMINE OXIDASE
Author
Yanwen Chen
Publisher
VDM Verlag Dr. Müller
Publication year
2010
Condition
Neu
Binding
Taschenbuch
Language
English
ISBN 10
3639255682
ISBN 13
9783639255683
Item weight
338 grams
Dimensions
220x176x33 mm

AHA-BUCH GmbH

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