Question

Arrange the steps of the mechanism of chymotrypsin catalysis in order from first to last?

1) Binding of substrate to the active site of chymotrypsin
2) Formation of an acyl-enzyme intermediate
3) Nucleophilic attack by water on the acyl-enzyme intermediate
4) Release of the cleaved peptide product

Answer 1

The correct sequence of steps in the mechanism of chymotrypsin catalysis starts with substrate binding to the active site, the formation of an acyl-enzyme intermediate, then a nucleophilic attack by water, concluding with the release of the peptide product.

Step-by-step explanation:

Chymotrypsin catalysis involves a specific sequence of steps that are essential for its enzymatic function. The mechanism of chymotrypsin catalysis begins with the binding of the substrate to its active site. This is followed by the formation of an acyl-enzyme intermediate, which then undergoes a nucleophilic attack by water, leading to the release of the cleaved peptide product. It's important to organize these steps in the correct sequence to understand the process fully.

1. Binding of substrate to the active site of chymotrypsin.
2. Formation of an acyl-enzyme intermediate.
3. Nucleophilic attack by water on the acyl-enzyme intermediate.
4. Release of the cleaved peptide product.