1. Chymotrypsin Chymotrypsin is one of the serine proteases.
Chymotrypsin is selective for peptide bonds with aromatic or large hydrophobic side chains, such as Tyr, Trp, Phe and Met, which are on the carboxyl side of this bond. It can also catalyze the hydrolysis of easter bond.
The main catalytic driving force for Chymotrypsin is the set of three amino acid known as catalytic triad. This catalytic pocket is found in the whole serine protease family.

2. Properties of an Active Site
A shape that fits a specific substrate or substrates only
Side chains that attract the enzyme particular substrate
Side chains specifically positioned to speed the reaction

3. The Catalytic Triad

5. Chymotrypsin Protein Hydrolysis
Stage #1

6. Chymotrypsin Protein Hydrolysis
Stage #2

7. Chymotrypsin Protein Hydrolysis
Stage #3

8. Chymotrypsin Protein Hydrolysis
Stage #4

9. Chymotrypsin Protein Hydrolysis
Stage #5

10. Chymotrypsin Protein Hydrolysis
Stage #6

11. Transition State Stabilization

13. Chymotrypsin Kinetics
The initial "burst" in
chymotrypsin-catalysed
hydrolysis of the p-nitrophenyl
acetate