Answer :
Option D-Asp 102 and His 57 from the B chain as well as Ser 195 from the C chain make up the active site of chymotrypsin.
Chymotrypsin (EC 3.4.21.1, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme that works in the duodenum to degrade proteins and polypeptides by a process called Chymotrypsin preferentially breaks peptide amide bonds when the side chain of the amino acid at the P1 position, which is N-terminal to the scissile amide bond, is a big hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids have an aromatic side chain that fits into an enzyme's hydrophobic pocket (the S1 location). When trypsin is present, it becomes active. The hydrophobic and form complementarity between the enzyme S1 binding cavity and the P1 side chain of the peptide substrate accounts for.
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Final answer:
The active site of chymotrypsin consists of a catalytic triad made up of Ser 195, His 57, and Asp 102, making option A correct.
Explanation:
The active site of chymotrypsin contains a catalytic triad, which is crucial for its function in cleaving peptide bonds. This catalytic triad is composed of three amino acids: Ser 195, His 57, and Asp 102. These three amino acids work together to carry out the biochemical reaction that cleaves peptide bonds, with His 57 acting as a general acid/base catalyst, Asp 102 increasing the basicity of His 57, and Ser 195 acting as a nucleophile. Therefore, the correct answer is A. Asp 102 and His57 from the A chain and Ser 195 from the C chain.
