Which enzyme activates trypsinogen to trypsin in the small intestine?

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Multiple Choice

Which enzyme activates trypsinogen to trypsin in the small intestine?

Explanation:
Activation of proteolytic enzymes in the small intestine begins when enteropeptidase, a brush-border enzyme from the duodenal mucosa, cleaves trypsinogen to form active trypsin. This activation starts the pancreatic zymogen cascade, because active trypsin then cleaves and activates other proenzymes such as chymotrypsinogen, proelastase, and procarboxypeptidases, enabling protein digestion. The other enzymes listed serve different roles: pancreatic amylase digests starches, lipase digests fats, and pepsin is a stomach enzyme that operates in acidic conditions and does not activate trypsinogen in the small intestine.

Activation of proteolytic enzymes in the small intestine begins when enteropeptidase, a brush-border enzyme from the duodenal mucosa, cleaves trypsinogen to form active trypsin. This activation starts the pancreatic zymogen cascade, because active trypsin then cleaves and activates other proenzymes such as chymotrypsinogen, proelastase, and procarboxypeptidases, enabling protein digestion. The other enzymes listed serve different roles: pancreatic amylase digests starches, lipase digests fats, and pepsin is a stomach enzyme that operates in acidic conditions and does not activate trypsinogen in the small intestine.

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