A small molecule that mimics the metabolic activity of copper-containing amine oxidases (CuAOs) toward physiological
Martine Largeron1, Maurice-Bernard Fleury, Margherita Strolin Benedetti
1UMR 8638 CNRS-Université Paris Descartes, Synthèse et Structure de Molécules d'Intérêt Pharmacologique, Faculté des Sciences Pharmaceutiques et Biologiques, 4 avenue de l'Observatoire, 75270 Paris cedex 06, France. martine.largeron@parisdescartes.fr
Abstract:
Primary aliphatic biogenic amines have been successfully oxidized using a quinonoid species that mimics the metabolic activity of copper-containing amine oxidase (CuAO) enzymes. Especially, high catalytic performances were observed with aminoacetone, a threonine catabolite, and methylamine, a metabolite of adrenaline, and with the primary amino groups of putrescine and spermidine which are both decarboxylation products of ornithine and S-adenosyl-methionine. Furthermore, contrary to flavine adenine dinucleotide (FAD)-dependent amine oxidase enzymes, no activity was found toward secondary and tertiary amines.
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