NVS- 2025
Biochemistry & Nutrition
Easy

The key enzyme that converts trypsinogen to trypsin is?

Appeared in: NVS- 2025

Explanation

  • Enteropeptidase (also called enterokinase) is the specific enzyme responsible for the initial conversion of inactive trypsinogen to active trypsin.
  • It is located on the brush border of the duodenal mucosa, ensuring activation occurs only within the small intestine.
  • This activation is the first and most critical step in a cascade that activates all other pancreatic proteolytic enzymes.
  • Once a small amount of trypsin is formed, it can then activate other zymogens, including more trypsinogen, chymotrypsinogen, and proelastase.

Why Other Options Were Wrong

  • Option A: Elastase is a proteolytic enzyme, but it is secreted as an inactive zymogen (proelastase) and is activated by trypsin. It does not activate trypsinogen.
  • Option C: Secretin is a hormone, not an enzyme. Its primary role is to stimulate the pancreas to secrete a bicarbonate-rich fluid to neutralize stomach acid in the duodenum.
  • Option D: Chymotrypsin is another powerful proteolytic enzyme, but like elastase, it is secreted as an inactive zymogen (chymotrypsinogen) and is activated by trypsin. It does not activate trypsinogen.

Related Visual

A flowchart illustrating the pancreatic zymogen activation cascade. It should begin with enteropeptidase on the duodenal wall converting trypsinogen to trypsin. Arrows should th...
Clinical Relevance
  • Nursing practice connection: This is primarily an exam-oriented knowledge point with limited direct bedside application, so retain Enzymatic activation of pancreatic proteases in the digestive system as background academic context rather than a clinical decision trigger.
  • Understanding this activation pathway is fundamental to comprehending protein digestion and the pathophysiology of malabsorption syndromes.
  • The principle of secreting inactive zymogens is a key protective mechanism for the pancreas. Failure of this system leads to acute pancreatitis, where activated enzymes autodigest the gland.
  • A congenital deficiency of enteropeptidase is a rare genetic disorder that causes severe protein malabsorption and failure to thrive in infants because the entire proteolytic cascade cannot be initiated.
How to Approach the Question
  • First, identify the core of the question: it asks for the specific enzyme that starts the conversion of an inactive form (trypsinogen) to an active form (trypsin).
  • This is a factual recall question based on digestive physiology.
  • Analyze the options to differentiate their roles. Recognize that Secretin is a hormone, not an enzyme involved in this specific conversion, which makes it an unlikely answer.
  • Recall the sequence of protein digestion in the small intestine. Pancreatic enzymes are released as inactive precursors (zymogens) to prevent self-digestion of the pancreas.
  • Remember that there is a specific 'trigger' or 'starter' enzyme located in the intestine itself. This enzyme is Enteropeptidase.
  • Differentiate this initial activator from the enzymes that are activated later in the cascade (like Chymotrypsin and Elastase), which are themselves activated by trypsin.
Concept Tested & Keywords
  • Concept Tested: Enzymatic activation of pancreatic proteases in the digestive system.
  • Stem keywords: enzyme, converts, trypsinogen, trypsin
  • Lead-in keywords: is

Question ID

Q_ntrlVrCz7XSH73eXgI6N

Reference Book

E6 Harper's Illustrated Biochemistry2023 (pp 26-793 of 813) p. 74-76

E6 Physiology Guyton 4SAE Part 2A p. 174-176

Practise the full NVS- 2025

Attempt every question from this paper in a timed mock, then review the full solution for each one.