Petkov D D
Biochim Biophys Acta. 1978 Apr 12;523(2):538-41. doi: 10.1016/0005-2744(78)90057-8.
The substituent dependence for kcat/Km of trypsin anilide hydrolysis is consistent with a rate-limiting general acid-base catalysed breakdown of a tetrahedral intermediate. The formation and disappearance of this intermediate during the hydrolysis of alpha-N-acetyl-L-lysin p-nitroanilide is observed in stopped-flow experiments.
胰蛋白酶催化苯胺水解反应的催化常数与米氏常数之比(kcat/Km)对取代基的依赖性,与四面体中间体通过限速的一般酸碱催化分解的情况相符。在α-N-乙酰-L-赖氨酸对硝基苯胺水解过程中该中间体的形成和消失,在停流实验中得以观察。