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.
利用一种模拟含
铜胺氧化酶(CuAO)代谢活性的
醌类物质,成功地氧化了初级脂肪族
生物胺。特别是对苏
氨酸的代谢产物
氨基
丙酮、
肾上腺素的代谢产物
甲胺以及
鸟氨酸和
S-腺苷蛋氨酸的脱羧产物
腐胺和
精胺的初级
氨基都有很高的催化性能。此外,与依赖
黄嘌呤腺嘌呤二核苷酸(FAD)的胺氧化酶相反,这种酶对仲胺和叔胺没有活性。