Transcript Chymotrypsin - New Jersey Medical School

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.
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
The Catalytic Triad
Chymotrypsin Protein Hydrolysis
Stage #1
Chymotrypsin Protein Hydrolysis
Stage #2
Chymotrypsin Protein Hydrolysis
Stage #3
Chymotrypsin Protein Hydrolysis
Stage #4
Chymotrypsin Protein Hydrolysis
Stage #5
Chymotrypsin Protein Hydrolysis
Stage #6
Transition State Stabilization
Chymotrypsin Kinetics
The initial "burst" in
chymotrypsin-catalysed
hydrolysis of the p-nitrophenyl
acetate