Multiple Choice
Why are most digestive enzymes produced as zymogens?
7. Enzyme Inhibition and Regulation
Zymogens
Struggling with Biochemistry?
Join thousands of students who trust us to help them ace their exams!Watch the first videoMultiple Choice
Which of the following is a zymogen that can be converted to a peptidase that hydrolyzes peptide bonds adjacent to lysine and arginine?
A
Chymotrypsin.
B
Pepsin.
C
Pepsinogen.
D
Trypsin.
E
Trypsinogen.
F
Proelastase.
Verified step by step guidance1
Understand the concept of a zymogen: A zymogen is an inactive precursor of an enzyme, which requires a biochemical change to become an active enzyme. This change often involves the cleavage of specific peptide bonds.
Identify the function of the active enzyme: The problem specifies that the active enzyme hydrolyzes peptide bonds adjacent to lysine and arginine. This is a characteristic function of the enzyme trypsin.
Recall the zymogen form of trypsin: The zymogen form of trypsin is trypsinogen. It is converted into active trypsin through the cleavage of specific peptide bonds, typically by the enzyme enteropeptidase in the small intestine.
Eliminate other options: Chymotrypsin, pepsin, and elastase are enzymes with different specificities and zymogen forms. For example, chymotrypsinogen is the zymogen form of chymotrypsin, and pepsinogen is the zymogen form of pepsin.
Conclude that trypsinogen is the correct zymogen: Based on the specificity for lysine and arginine and the known zymogen forms, trypsinogen is the zymogen that converts to trypsin, which hydrolyzes peptide bonds adjacent to these amino acids.
Related Videos
Related Practice
