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Trypsin-like serine proteases are a major subgroup of serine proteases characterized by their substrate specificity for cleaving after lysine or arginine residues. They possess a conserved catalytic triad (Ser195-His57-Asp102) and are involved in diverse physiological processes including digestion, coagulation, and immunity. These enzymes are classified within MEROPS Clan PA, Family S1. Inhibitors and activity-based probes are used for research and therapeutic purposes.
Inhibition of serine protease activity via binding to the active site, preventing substrate binding and peptide bond cleavage.
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