Serine Protease (Trypsin) (None)

Serine proteases are a large family of enzymes characterized by a serine residue in their active site, which is essential for their catalytic function. Trypsin is one of the most well-known members of this family. It catalyzes the hydrolysis of peptide bonds on the carboxyl side of lysine or arginine residues and plays a critical role in protein digestion. It is secreted as an inactive precursor called trypsinogen and activated in the small intestine. Trypsin is also involved in activating other digestive enzymes and has roles in blood coagulation and immune responses.

Other names

Trypsin

Hydrolyzes peptide bonds at the carboxyl side of lysine or arginine residues; inhibited by serine protease inhibitors.