Final answer:
Chymotrypsin achieves substrate specificity through its unique active site tailored to aromatic amino acids and the induced fit mechanism, allowing slight adaptation of shape to fit the substrate optimally.
Step-by-step explanation:
Chymotrypsin achieves substrate specificity through the unique structure of its active site. The amino acids within this active site create a specific chemical environment suitable for binding to particular substrates—namely, aromatic amino acids like phenylalanine, tyrosine, and tryptophan. This specificity is a result of the shape and properties of the enzyme's side chains, which match the substrate much like a jigsaw puzzle. Additionally, the mechanism of induced fit allows the enzyme to adapt its shape slightly to form the best possible fit with the substrate's transition state, further enhancing specificity. While chymotrypsin is primarily specific to aromatic amino acids, enzymes, in general, may have some flexibility and can sometimes act on several structurally related substrates.