Chymotrypsin cleaves peptide bonds by attacking the unreactive carbonyl group with a powerful nucleophile, the serine 195 residue located in the active site of the enzyme, which briefly becomes covalently bonded to the substrate, forming an enzyme-substrate intermediate.
These findings rely on inhibition assays and the study of the kinetics of cleavage of the aforementioned substrate, exploiting the fact that the enzyme-substrate intermediate p-nitrophenolate has a yellow colour, enabling us to measure its concentration by measuring light absorbance at 405 nm.
It was found that the reaction of chymotrypsin with its substrate takes place in two stages, an initial “burst” phase at the beginning of the reaction and a steady-state phase following Michaelis-Menten kinetics.It is also called "ping-pong" mechanism. The mode of action of chymotrypsin explains this as hydrolysis takes place in two steps. First acylation of the substrate to form an acyl-enzyme intermediate and then deacylation in order to return the enzyme to its original state.
Chymotrypsin-Like Protease Activity in the Stratum Corneum Is Increased in Atopic Dermatitis and upon Washing with Soap
Oct 01, 2013; A critical event in the development of atopic dermatitis is breakdown of the skin barrier formed by the intact stratum corneum....
A dimeric high-molecular-weight chymotrypsin inhibitor with antitumor and HIV-1 reverse transcriptase inhibitory activities from seeds of Acacia confusa.(Report)
Jul 01, 2010; ABSTRACT A dimeric 70-kDa chymotrypsin inhibitor with substantial N-terminal sequence homology to serine protease...