PMID: 9428687Jan 15, 1998Paper

Tryptamine as substrate and inhibitor of lentil seedling copper amine oxidase

European Journal of Biochemistry
Rosaria MeddaGiovanni Floris

Abstract

Copper amine oxidase from lentil seedlings was shown to be able to catalyze the oxidative deamination of the indoleamines tryptamine, 5-hydroxytryptamine, and 5-methoxytryptamine. These compounds showed saturation kinetics with Km values as normal substrates, but their oxidation led to irreversible loss of enzyme activity suggesting a covalent interaction with the enzyme, most probably through its cofactor 6-hydroxydopa (2,4,5-trihydroxyphenylalanine). These indoleamines acted as irreversible inhibitors of the enzyme only in the absence of oxygen but they brought about changes in the electronic spectra of the enzyme both in aerobiosis and in anaerobiosis. This study reports on the mechanism by which these compounds inhibit lentil amine oxidase which involves first the oxidation of indoleamines bound to 6-hydroxydopa followed by the formation of an irreversible covalent derivative. The same inhibitory mechanism could possibly lead to inactivation of mammalian amine oxidases involved in serotonin neurotransmitter metabolism in conditions of ischemia or hypoxia.

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Citations

Dec 23, 2003·European Journal of Biochemistry·Paola PietrangeliLaura Morpurgo
May 12, 2004·Biological Chemistry·Alessandra PadigliaRosaria Medda
Jul 24, 2010·Plant Physiology and Biochemistry : PPB·Marcel AribaudIsabelle Fock
Feb 10, 2009·Plant Physiology and Biochemistry : PPB·Marcel AribaudHippolyte Kodja
Aug 2, 2005·Phytochemistry·Silvia LonguGiovanni Floris
Jul 14, 1999·FEBS Letters·R MeddaG Floris
Oct 30, 1998·Journal of Enzyme Inhibition·A PadigliaG Floris

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