Broad-spectrum serine protease

Broad-spectrum serine proteases are a diverse group of enzymes characterized by a nucleophilic serine residue in their active site that facilitates the cleavage of peptide bonds in proteins (NCBI, NBK22571). These enzymes play critical roles in a wide array of physiological processes, including digestion, blood coagulation, fibrinolysis, and the immune response (UniProt). In various disease states, such as pancreatitis, cancer, and viral infections, the dysregulation or hijacking of these proteases contributes significantly to pathogenesis (PubMed, PMID: 28257286). For instance, host serine proteases like TMPRSS2 are essential for the proteolytic priming of viral spike proteins, enabling the entry of viruses like SARS-CoV-2 into host cells (PubMed, PMID: 32142651). Drugs targeting this broad class, such as camostat and nafamostat, act by inhibiting the enzymatic activity across multiple members of the family, offering therapeutic potential in treating inflammatory conditions and preventing viral replication (PubChem, CID: 2536). However, the lack of specificity can lead to challenges in maintaining the balance of homeostatic processes like coagulation (StatPearls, NBK541041).

Other names

Serine proteaseSerine endopeptidaseSerine hydrolaseSerine-type peptidaseSerine protease family

Broad-spectrum serine protease inhibitors typically function by forming a reversible or irreversible complex with the catalytic serine residue in the enzyme's active site, thereby blocking the substrate from binding and preventing proteolysis (NCBI, NBK22571; PubMed, PMID: 32142651).