Multiple Choice
Why are most digestive enzymes produced as zymogens?
7. Enzyme Inhibition and Regulation
Zymogens
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How is chymotrypsinogen converted to chymotrypsin?
A
A protein kinase-catalyzed phosphorylation converts chymotrypsinogen to chymotrypsin.
B
An increase in [Ca2+] promotes the conversion.
C
Proteolysis of chymotrypsinogen forms chymotrypsin.
D
Two inactive chymotrypsinogen dimers pair to form an active chymotrypsin tetramer.
Verified step by step guidance1
Chymotrypsinogen is an inactive zymogen, which is a precursor to an active enzyme.
The conversion of chymotrypsinogen to chymotrypsin involves proteolytic cleavage, which is a process where specific peptide bonds in the zymogen are hydrolyzed.
This proteolysis is typically catalyzed by another enzyme, such as trypsin, which cleaves chymotrypsinogen at specific sites to activate it.
The cleavage results in a conformational change that allows the active site of the enzyme to be properly formed, thus activating chymotrypsin.
The active chymotrypsin can then participate in the digestion of proteins by cleaving peptide bonds at specific amino acid residues.
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