Detection of a tetrahedral intermediate in the trypsin-catalysed hydrolysis of specific ring-activated anilides.
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.
D000813:Anilides; D000818:Animals; D002417:Cattle; D007700:Kinetics; D008433:Mathematics; D011485:Protein Binding; D013379:Substrate Specificity; D014357:Trypsin / Q000378:metabolism*
D000813:Anilides; D014357:Trypsin