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Procoagulant Adaptation of a Blood Coagulation Prothrombinase-like Enzyme Complex in Australian Elapid Venom

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Author(s): Mettine H.A. Bos | Rodney M. Camire

Journal: Toxins
ISSN 2072-6651

Volume: 2;
Issue: 6;
Start page: 1554;
Date: 2010;
Original page

Keywords: snake venom | blood coagulation | prothrombinase complex | factor X | factor V | prothrombin activation | serine protease | hemostatic toxin

ABSTRACT
The macromolecular enzyme complex prothrombinase serves an indispensable role in blood coagulation as it catalyzes the conversion of prothrombin to thrombin, a key regulatory enzyme in the formation of a blood clot. Interestingly, a virtually identical enzyme complex is found in the venom of some Australian elapid snakes, which is composed of a cofactor factor Va-component and a serine protease factor Xa-like subunit. This review will provide an overview of the identification and characterization of the venom prothrombinase complex and will discuss the rationale for its powerful procoagulant nature responsible for the potent hemostatic toxicity of the elapid venom.