Question

What are the steps in the mechanism of chymotrypsin catalysis?

1) Substrate binding
2) Formation of acyl-enzyme intermediate
3) Hydrolysis of the acyl-enzyme intermediate
4) Release of the products

Answer 1

The mechanism of chymotrypsin catalysis involves substrate binding, formation of acyl-enzyme intermediate, hydrolysis of the acyl-enzyme intermediate, and release of the products.

Step-by-step explanation:

The steps in the mechanism of chymotrypsin catalysis are as follows:

1. Substrate binding: The substrate binds to the active site of the enzyme through hydrogen bonding and other electrostatic interactions.
2. Formation of acyl-enzyme intermediate: As the substrate binds, the enzyme undergoes conformational changes, straining the shape of the active site and distorting the substrate, forming an acyl-enzyme intermediate.
3. Hydrolysis of the acyl-enzyme intermediate: In this step, water molecules attack the acyl-enzyme intermediate, breaking the bond between the enzyme and the substrate and forming new bonds with the products.
4. Release of the products: The products of the reaction are released from the active site, allowing the enzyme to catalyze another reaction.