Chymotrypsinogen is converted to chymotrypsin by which enzyme?

Chymotrypsinogen is a zymogen, an inactive precursor of the enzyme chymotrypsin. Its activation is crucial for protein digestion in the small intestine. The specific enzyme responsible for converting chymotrypsinogen to its active form, chymotrypsin, is trypsin.

Trypsin itself is activated from its zymogen form, trypsinogen, primarily by enterokinase, an enzyme produced in the intestinal mucosa. Once activated, trypsin can then catalyze the conversion of chymotrypsinogen into chymotrypsin by cleaving specific peptide bonds in the zymogen, thereby transforming it into an active enzyme capable of participating in protein digestion.

This conversion is a critical step in the digestion process because it allows for the breakdown of dietary proteins into peptides and amino acids, which are then absorbed by the body. The specificity of trypsin in activating other digestive proteases underscores its essential role in the overall digestive enzyme cascade.