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Fibrinolytic enzymes are a broad class of proteolytic enzymes that catalyze the degradation of fibrin, the primary protein component of blood clots. Members include both endogenous enzymes (such as plasmin and its activators, tissue plasminogen activator and urokinase) and exogenous enzymes obtained from bacteria (streptokinase, staphylokinase), animals (lumbrokinase), and plants (nattokinase, bromelain, serrapeptase). These enzymes are used therapeutically to dissolve blood clots in a range of cardiovascular conditions, including myocardial infarction, stroke, and pulmonary embolism. Their mechanisms involve either direct proteolysis of fibrin or activation of the body's own plasminogen system; selectivity and safety profiles vary among agents. Excessive activation of fibrinolysis can lead to serious bleeding events, representing the main clinical safety concern. Notes on correctness: "Fibrinolytic enzymes" refers to a class/category, not a unique molecular target, and may group together distinct proteins such as plasmin, tPA, and a range of microbial and plant-derived enzymes. Individual drugs and biomarkers often act on or mimic one principal endogenous enzyme (e.g., plasmin), not the entire class. This imprecision makes "Fibrinolytic enzymes" too generic as a single drug target entry. For structured pharmacological databases, each specific enzyme (e.g., "Tissue plasminogen activator", "Streptokinase", "Nattokinase") should be entered separately, with "Fibrinolytic enzyme" serving as a broader functional category, not a canonical target.
Catalysis of fibrin degradation (direct breakdown of fibrin mesh); Activation of plasminogen to plasmin (indirectly increasing endogenous fibrinolysis); Enhancement of tissue plasminogen activator (tPA) activity; Non-selective proteolysis (for some agents)
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