Molecular Classification
Enzyme, Protease, Serine Protease, Serine endopeptidase
Disease Roles
Malabsorption (indirectly)Pancreatic insufficiency (indirectly)Cystic fibrosis (indirectly)

Chymotrypsin Overview

Chymotrypsin is a serine protease enzyme primarily involved in the digestion of proteins in the small intestine. It catalyzes the hydrolysis of peptide bonds, specifically those adjacent to aromatic amino acids such as phenylalanine, tryptophan, and tyrosine. It is synthesized in the pancreas as an inactive precursor (chymotrypsinogen) and activated in the digestive tract.

Mechanism of Action

Covalent hydrolysis of peptide bonds adjacent to aromatic amino acids (Phe, Trp, Tyr) via acyl-enzyme intermediate formation.

Biological Functions

Proteolysis
Protein digestion

Disease Associations

Malabsorption (indirectly)
Pancreatic insufficiency (indirectly)
Cystic fibrosis (indirectly)

Safety Considerations

  • Potential for off-target proteolysis
  • Autolysis and instability under certain conditions
  • Inhibition by heavy metals

Interacting Drugs

Protease inhibitors (general)
Heavy metals (Cu2+, Hg2+)