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Chymotrypsin is a serine protease enzyme that catalyzes the hydrolysis of peptide bonds in proteins, specifically those adjacent to aromatic amino acids such as phenylalanine, tyrosine, and tryptophan. It is secreted by the pancreas as an inactive zymogen called chymotrypsinogen and is activated in the small intestine by proteolytic cleavage. The catalytic mechanism of chymotrypsin involves a two-step process known as acylation and deacylation, which together constitute a ping-pong bi-bi mechanism. The active site of chymotrypsin contains a catalytic ________ ________ _______ __________ ____ _________ _______.
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