Question

Where is chymotrypsin produced?

Answer 1

Chymotrypsin:

1. In the pancreas, chymotrypsin is produced as an inactive precursor known as chymotrypsinogen.
2. The three polypeptide molecule active chymotrypsin that results from cleavage is joined by disulphide linkages.
3. In the small intestine, chymotrypsin catalyzes the breakdown of protein peptide bonds.
4. Additionally, chymotrypsin facilitates the hydrolysis of ester bonds.
5. It is selective to peptide bonds that have large hydrophobic or aromatic side chains on the carboxyl end of the bond.
6. It is a serine protease.
7. Chymotrypsin breaks down peptide bonds by attacking the inert carbonyl group with a potent nucleophile.
8. This nucleophile is the Ser¹⁹⁵(serine) residue in the enzyme's active site, which momentarily links covalently to the substrate to create an enzyme-substrate intermediate.