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.
AKTIFASI CHYMOTRYPSINOGEN
 Chymotrypsin Kinetics

The initial "burst" in

chymotrypsin-catalysed
hydrolysis of the p-nitrophenyl
acetate
Perbedaan Spesifik Chymotrypsin, Trypsin, and Elastase
• Substrate specificity
– Chymotrypsin: aromatic or bulky nonpolar side chain
– Trypsin: Lys or Arg
– Elastase: smaller & uncharged side chains
• Small structural difference in the binding site explains the
substrate specificity

nonpolar pocket Asp (negatively charged) no pocket present

vs. Ser in Chymotrypsin as two Gly in chymotrypsin
are replaced by Val and Thr