Chymotrypsinogen Chymotrypsin. (inactive) Made as an inactive precursor 245 (chymotrypsinogen)in the pancreas. Trypsin Activation by cleavage of the peptide -Chymotrypsin (active) bond between Arg-15 and lle-16 with trypsin->n-chymotrypsin;cleavage 15 16 245 results in a small conformational change with large consequences Chymotrypsin ·π-Chymotrypsin removes2 dipeptides (residues 14-15 and 147-148)from other a-Chymotrypsin Two dipeptides n-chymotrypsin molecules->a- (active) chymotrypsin.Activity does not change 1 13 16 146 149 245 after this second proteolytic step: chymotrypsin is already fully active. A chain B chain C chain Chymotrypsin. • Made as an inactive precursor (chymotrypsinogen) in the pancreas. • Activation by cleavage of the peptide bond between Arg-15 and Ile-16 with trypsin -> -chymotrypsin; cleavage results in a small conformational change with large consequences ! • -Chymotrypsin removes 2 dipeptides (residues 14-15 and 147-148) from other -chymotrypsin molecules -> - chymotrypsin. Activity does not change after this second proteolytic step: - chymotrypsin is already fully active