9 Questions
Which enzyme converts pancreatic zymogen TRYPSINOGEN to TRYPSIN?
Enteropeptidase
What is the role of TRYPSIN in the activation of other pancreatic zymogens?
It is the common activator of all pancreatic zymogens
Which amino acids contribute to the peptide bond cleaved by TRYPSIN?
Arginine and Lysine
What is the function of aminopeptidase on the luminal surface of the intestine?
It repeatedly cleaves the N-terminal residue from oligopeptides
Which enzyme converts trypsinogen to trypsin?
Elastase
What is the role of Enteropeptidase in the activation cascade of proteolytic enzymes?
Activates all pancreatic zymogens by converting trypsinogen to trypsin
Which enzyme has specificity for amino acid R-groups adjacent to susceptible peptide bonds?
Chymotrypsin
Which enzyme specifically cleaves when the carbonyl group of the peptide bond is contributed by Arginine or Lysine?
{Trypsin}
'Aminopeptidase' is responsible for cleaving which part of oligopeptides?
N-terminal residue
Learn about the activation of pepsinogen to pepsin by HCl or autocatalytically, the optimum pH range for pepsin activity, and how pepsin releases peptides and amino acids from dietary proteins. Dive into the history of Pepsi as an interesting side fact.
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