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Exploring the Diversity and Function of Serine Proteases in Toxicofera Reptile Venoms: A Comprehensive Overview
Julia F D Vidal1, Matheus F Schwartz1, Aisel V Garay1
1Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Brasília, Asa Norte, Brasilia 70910-900, DF, Brazil.
Abstract:
Toxicofera reptile venoms are composed of several toxins, including serine proteases. These proteases are glycosylated enzymes that affect the prey's hemostatic system. Their actions extend across the coagulation cascade, the kallikrein-kinin system, and platelet activation. Despite their specificity for different substrates, these enzymes are homologous across all toxicoferans and display high sequence similarity. The aim of this review is to compile decades of knowledge about venom serine proteases, showing the diversity of biochemically and biophysically characterized enzymes, their structural characteristics, advances in understanding their origin and evolution, as well as methods of obtaining enzymes and their biotechnological applications.
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