Chymotrypsin is a digestive enzyme that is secreted by the pancreas. It belongs to the family of enzymes called serine proteases that includes trypsin. These proteins cleave proteins into smaller peptides, and the side chain of serine plays a catalytice role in this cleavage. Chymotrypsin hydrolyzes the peptide bond of amino acids with large hydrophobic side chains, such as phenylalanine, tryptophan, and tyrosine.
Explore the structural aspects of chymotrypsin's enzymatic action below!
Chymotrypsin consists of 3 chains, A (Blue), B (Aqua), and C (Green). It is derived from the precursor chymotrypsinogen, which is 245 amino acid residues long. The three separate chains of the activated chymotrypsin are formed when two dipeptide units, consisting of residues 14 and 15 and residues 147 and 148 are removed. Click