Foppoli C, Coccia R, Blarzino C
Ital J Biochem. 1986 Nov-Dec;35(6):385-90.
S-(1-carboxyethyl)-L-cysteine (1-CEC) and S-(1-carboxypropyl)-L-cysteine (1-CPC) are oxidatively deaminated by L-aminoacid oxidase with consumption of half a mole of oxygen per mole of substrate in the presence of catalase. This reaction gives rise to the corresponding alpha-ketoacids, identified by some chemical and chromatographic tests and by comparison with synthetic compounds. It has been possible, therefore, to demonstrate that S-(1-carboxyethyl)-thiopvruvic acid (1-CETP) and S-(1-carboxypropyl)-thiopvruvic acid (1-CPTP) are the main products of oxidative deamination of 1-CEC and 1-CPC.
S-(1-羧乙基)-L-半胱氨酸(1-CEC)和S-(1-羧丙基)-L-半胱氨酸(1-CPC)在过氧化氢酶存在的情况下，被L-氨基酸氧化酶氧化脱氨，每摩尔底物消耗半摩尔氧气。该反应产生相应的α-酮酸，通过一些化学和色谱测试以及与合成化合物比较得以鉴定。因此，已经能够证明S-(1-羧乙基)-硫代丙酮酸(1-CETP)和S-(1-羧丙基)-硫代丙酮酸(1-CPTP)是1-CEC和1-CPC氧化脱氨的主要产物。
