A small molecule that mimics the metabolic activity of copper-containing amine oxidases (CuAOs) toward physiological mono- and polyamines

Martine Largeron (1, 2) , Maurice-Bernard Fleury (3) , Margherita Strolin Benedetti

1 CiTCoM - UMR 8038 - Cibles Thérapeutiques et conception de médicaments
2 CiTCoM - UMR 8038 - Cibles Thérapeutiques et conception de médicaments
3 SSMIP - Synthèse et structure de molécules d'interet pharmacologique

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, both decarboxylation products of ornithine and S-adenosylmethionine. Furthermore, contrary to flavine adenine dinucleotide (FAD)-dependent amine oxidase enzymes, no activity was found toward secondary and tertiary amines.

Domaines: Catalyse; Chimie organique; Chimie théorique et/ou physique

Martine Largeron, Maurice-Bernard Fleury, Margherita Strolin Benedetti. A small molecule that mimics the metabolic activity of copper-containing amine oxidases (CuAOs) toward physiological mono- and polyamines. Organic & Biomolecular Chemistry, 2010, 8 (16), pp.3796. ⟨10.1039/c004501b⟩. ⟨hal-02384876⟩