Proteases are enzymes that catalyze the hydrolysis of peptide bonds, cleaving proteins and Peptides into smaller fragments or single amino acids. They are classified by the catalytic residue or mechanism at their active site into serine, cysteine, aspartic, threonine, and metalloproteases, and by whether they cleave…
Proteases are enzymes that catalyze the hydrolysis of peptide bonds, cleaving proteins and Peptides into smaller fragments or single amino acids. They are classified by the catalytic residue or mechanism at their active site into serine, cysteine, aspartic, threonine, and metalloproteases, and by whether they cleave internal bonds, as endopeptidases, or remove terminal residues, as exopeptidases. Far from simple degradative enzymes, proteases regulate biology through precise, often irreversible cleavage events. They drive digestion, activate and inactivate hormones and signaling molecules, control the blood coagulation cascade through sequential activation of clotting factors, mediate immune responses, and remodel the extracellular matrix during tissue repair and wound healing. Their activity is tightly regulated by zymogen activation, inhibitors, and compartmentalization, because uncontrolled proteolysis is damaging; imbalance between proteases and their inhibitors contributes to impaired wound healing, bleeding and clotting disorders, and disease progression. Proteomic methods are used to catalogue proteases and their substrates and to study their roles in health and disease. Beyond physiology, proteases have wide industrial and therapeutic applications, from food and detergent processing to pharmaceuticals. Research in this area addresses protease function in coagulation and wound repair, proteomic characterization of proteins and their processing, and the regulation of proteolytic activity in normal and pathological states.
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