Page "Chymotrypsin" Paragraph 3

In vivo, chymotrypsin is a proteolytic enzyme ( Serine protease ) acting in the digestive systems of mammals and other organisms.

It facilitates the cleavage of peptide bonds by a hydrolysis reaction, which despite being thermodynamically favourable occurs extremely slowly in the absence of a catalyst.

The main substrates of chymotrypsin include tryptophan, tyrosine, phenylalanine, leucine, and methionine, which are cleaved at the carboxyl terminal.

Like many proteases, chymotrypsin will also hydrolyse amide bonds in vitro, a virtue that enabled the use of substrate analogs such as N-acetyl-L-phenylalanine p-nitrophenyl amide for enzyme assays.