Exploring the Diversity and Function of Serine Proteases in Toxicofera Reptile Venoms: A Comprehensive Overview

• Published in: Toxins Vol. 16; no. 10; p. 428
• Main Authors: Vidal, Julia F D, Schwartz, Matheus F, Garay, Aisel V, Valadares, Napoleão F, Bueno, Renata V, Monteiro, Ana Carolina L, Freitas, Sônia Maria de, Barbosa, João Alexandre R G
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 03-10-2024; MDPI
• Subjects: Analysis; Animals; Biotechnology; Coagulation; coagulation cascade; Composition; Enzymes; Glycoproteins; hemostasis-affecting toxins; Humans; Identification and classification; kallikrein–kinin system; Peptides; Proteases; Proteins; Reptiles; Review; Serine Proteases - metabolism; Serine proteinase; snake venom serine protease; Snakes; Toxicofera venom evolution; Toxins; Venom; venom toxin; Brazil; snake venom serine protease; coagulation cascade; kallikrein–kinin system; Toxicofera venom evolution; hemostasis-affecting toxins; venom toxin; platelet activation
• ISSN: 2072-6651; 2072-6651
• DOI: 10.3390/toxins16100428

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.