A small molecule that mimics the metabolic activity of copper-containing amine oxidases (CuAOs) toward physiological mono- and polyamines.
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.
Largeron
Martine
M
UMR 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
Fleury
Maurice-Bernard
MB
Strolin Benedetti
Margherita
M
D006631:Amine Oxidase (Copper-Containing) / Q000378:metabolism*; D000588:Amines / Q000737:chemistry* / Q000378:metabolism*; D055162:Biocatalysis; D040761:Biomimetic Materials / Q000737:chemistry* / Q000378:metabolism*; D015394:Molecular Structure; D010084:Oxidation-Reduction; D011073:Polyamines / Q000737:chemistry* / Q000378:metabolism*; D013379:Substrate Specificity
D000588:Amines; D011073:Polyamines; D006631:Amine Oxidase (Copper-Containing)