Answer :
Enzyme Active Sites and their Reaction Mechanisms, Harry Morrison, 2021 α - The "hydrolytic enzyme" chymotrypsin (EC 3.4.21.1; chymotrypsinogen .
A) belongs to the superfamily of serine proteases and hydrolyzes peptide bonds by using a serine hydroxyl group as a nucleophile in the active site. The pancreas is where chymotrypsin is largely made. To stop its protease activity from dissolving the pancreas, it is created as the inactive zymogen chymotrypsinogen rather than the active version. A different enzyme known as trypsin changes it into its active form when it is secreted into the lumen of the small intestine.
Trypsin is the primary enzyme that breaks down chymotrypsin, which is also known as chymotrypsinogen. Active enzymes can occasionally even cleave the incoming inactive form of themselves.
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Final answer:
The active site of chymotrypsin comprises Asp 102 and His57 from the A chain, and Ser 195 from the C chain.
Explanation:
The active site of chymotrypsin, an important enzyme in digestion, consists of three amino acids: Asp 102, His 57, and Ser 195. This is a part of the catalytic triad commonly found in a number of hydrolases. These three amino acids are spread across different chains in the chymotrypsin molecule. The correct combination is: Asp 102 and His57 are from the A chain, and Ser 195 is from the C chain. So, the first option is correct.
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