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Biochemistry · Proenzymes: digestive protease activation
Sample itemDuodenal fluid from an infant with protein malabsorption and oedema has very low trypsin and chymotrypsin activity. Adding enteropeptidase restores activity. Which statement describes the normal role of this enzyme?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
C. It cleaves trypsinogen to trypsin, which then activates the other pancreatic zymogens
Enteropeptidase (enterokinase) is a brush border enzyme of the duodenum that removes an N-terminal activation peptide from trypsinogen. Trypsin then activates chymotrypsinogen, proelastase, procarboxypeptidases and more trypsinogen. Congenital deficiency causes diarrhoea, failure to thrive and hypoproteinaemia.
Option by option
A. It converts procarboxypeptidase to trypsin directly
Procarboxypeptidase is activated by trypsin, and enteropeptidase does not form trypsin from it.
B. It activates pepsinogen in the stomach
Pepsinogen is activated by gastric acid and by pepsin itself.
C. It cleaves trypsinogen to trypsin, which then activates the other pancreatic zymogens (correct)
Correct. Enteropeptidase starts the zymogen cascade by generating trypsin.
D. It cleaves dietary lactose at the brush border
Lactose is cleaved by lactase, not by enteropeptidase.
Source note: Original NextPrep sample item — pending expert review. This item is original practice material awaiting independent expert review, so confirm important facts in a standard textbook.
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