Question

The active site of chymotrypsin consists of a catalytic triad of which of the following amino acid residues?

• A. \( \text{Serine, histidine, and glutamate} \)
• B. \( \text{Threonine, histidine, and aspartate} \)
• C. \( \text{Serine, histidine, and aspartate} \)
• D. \( \text{Methionine, histidine, and aspartate} \)

Hint:

The catalytic triad in chymotrypsin facilitates hydrolysis by activating serine for nucleophilic attack.

Answer 1

The Correct Option is C

Chymotrypsin, a serine protease, contains a catalytic triad of serine, histidine, and aspartate, which enables protein cleavage. Histidine acts as a proton acceptor, serine provides nucleophilic attack, and aspartate stabilizes the charge. This arrangement is essential for the enzyme’s proteolytic function in breaking peptide bonds.