Chymotrypsin-like serine protease

Chymotrypsin-like serine protease is a member of the serine protease superfamily characterized by a highly conserved active site serine and a preference for cleaving peptide bonds following large hydrophobic amino acids such as phenylalanine, tryptophan, and tyrosine[1][2][3]. The canonical example is chymotrypsin, a digestive enzyme secreted by the pancreas, but this group comprises a large family including enzymes involved in digestion, blood coagulation, immunity, and viral protein processing[2][3][6][7]. These proteases function by using the nucleophilic serine in the catalytic triad to facilitate peptide bond hydrolysis and are involved in various physiological and pathological processes, ranging from protein digestion in the gut to activation of viral polyproteins in viruses such as SARS-CoV-2[1][2][3][6][7]. Owing to their central roles, they are important therapeutic targets for enzyme inhibitors (including antiviral drugs and anti-inflammatory agents), and their dysregulation is implicated in disease processes such as cancer, inflammation, infection, and neurodegeneration[2][3][4][7].

Other names

Chymotrypsin-like proteaseChymotrypsin-clan serine protease3-chymotrypsin-like protease (in viruses, e.g., 3CLpro)Chymotrypsin-like enzyme

Covalent active site inhibition (serine-modifying inhibitory drugs form covalent adducts) Competitive inhibition (small molecules block the substrate pocket) Irreversible inhibition (serpins, pharmaceuticals)