Pepsin Enzyme Function and Activation
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Questions and Answers

Which enzyme converts pancreatic zymogen TRYPSINOGEN to TRYPSIN?

  • Chymotrypsinogen
  • Enteropeptidase (correct)
  • Elastase
  • Procarboxypeptidase

What is the role of TRYPSIN in the activation of other pancreatic zymogens?

  • It serves as a substrate for other zymogens
  • It inhibits the activation of zymogens
  • It is the common activator of all pancreatic zymogens (correct)
  • It plays no role in zymogen activation

Which amino acids contribute to the peptide bond cleaved by TRYPSIN?

  • Aspartic Acid and Glutamic Acid
  • Cysteine and Methionine
  • Arginine and Lysine (correct)
  • Phenylalanine and Tyrosine

What is the function of aminopeptidase on the luminal surface of the intestine?

<p>It repeatedly cleaves the N-terminal residue from oligopeptides (D)</p> Signup and view all the answers

Which enzyme converts trypsinogen to trypsin?

<p>Elastase (C)</p> Signup and view all the answers

What is the role of Enteropeptidase in the activation cascade of proteolytic enzymes?

<p>Activates all pancreatic zymogens by converting trypsinogen to trypsin (A)</p> Signup and view all the answers

Which enzyme has specificity for amino acid R-groups adjacent to susceptible peptide bonds?

<p>Chymotrypsin (B)</p> Signup and view all the answers

Which enzyme specifically cleaves when the carbonyl group of the peptide bond is contributed by Arginine or Lysine?

<p>{Trypsin} (C)</p> Signup and view all the answers

'Aminopeptidase' is responsible for cleaving which part of oligopeptides?

<p>N-terminal residue (B)</p> Signup and view all the answers

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