The only protease zymogen that could be converted to its active form in the absence of enteropeptidase is chymotripsinogen.
Trypsinogen is transformed into active trypsin by enteropeptidase, which also activates several pancreatic zymogens in addition to hydrolyzing a few peptide links in specific dietary proteins. Enteropeptidase is a crucial enzyme in the digestion of dietary proteins because of this, and its lack may cause severe protein malabsorption.
Trypsinogen, which is enteropeptidase's main substrate, undergoes a limited amount of proteolysis to release trypsin with catalytic activity. By limited proteolysis, trypsin then acts on the 4 other zymogens to release chymotrypsin, elastase, and carboxypeptidases A and B that are catalytically active.
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