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The broad spectrum serine protease plasmin is formed following cleavage of the zymogen precursor plasminogen by host activators tissue plasminogen activator and urokinase.
Substitution of Glu 351 also altered the specificity toward non-cognate proteases: plasmin and thrombin.
Degradation of fibrin clots is the function of plasmin , a serine protease that circulates as the inactive proenzyme, plasminogen.
Plasminogen activators attached to fibrin activate plasminogen, causing the release of the enzyme plasmin within clots and thrombi.
The fibrinolytic system involves a series of enzymatic reactions that results in the conversion of the proenzyme, plasminogen, into the trypsin-like lyric enzyme, plasmin .
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