Exploring the Diversity and Function of Serine Proteases in Toxicofera Reptile Venoms: A Comprehensive Overview
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 speci...
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| Published in: | Toxins Vol. 16; no. 10; p. 428 |
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| Main Authors: | , , , , , , , |
| Format: | Journal Article |
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| 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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| AbstractList | 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.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. 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. |
| Audience | Academic |
| Author | Monteiro, Ana Carolina L Valadares, Napoleão F Freitas, Sônia Maria de Barbosa, João Alexandre R G Bueno, Renata V Garay, Aisel V Vidal, Julia F D Schwartz, Matheus F |
| AuthorAffiliation | Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Brasília, Asa Norte, Brasilia 70910-900, DF, Brazil |
| AuthorAffiliation_xml | – name: Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Brasília, Asa Norte, Brasilia 70910-900, DF, Brazil |
| Author_xml | – sequence: 1 givenname: Julia F D surname: Vidal fullname: Vidal, Julia F D organization: Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Brasília, Asa Norte, Brasilia 70910-900, DF, Brazil – sequence: 2 givenname: Matheus F surname: Schwartz fullname: Schwartz, Matheus F organization: Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Brasília, Asa Norte, Brasilia 70910-900, DF, Brazil – sequence: 3 givenname: Aisel V surname: Garay fullname: Garay, Aisel V organization: Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Brasília, Asa Norte, Brasilia 70910-900, DF, Brazil – sequence: 4 givenname: Napoleão F orcidid: 0000-0002-6251-7342 surname: Valadares fullname: Valadares, Napoleão F organization: Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Brasília, Asa Norte, Brasilia 70910-900, DF, Brazil – sequence: 5 givenname: Renata V orcidid: 0000-0002-9802-331X surname: Bueno fullname: Bueno, Renata V organization: Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Brasília, Asa Norte, Brasilia 70910-900, DF, Brazil – sequence: 6 givenname: Ana Carolina L surname: Monteiro fullname: Monteiro, Ana Carolina L organization: Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Brasília, Asa Norte, Brasilia 70910-900, DF, Brazil – sequence: 7 givenname: Sônia Maria de orcidid: 0000-0002-7562-4980 surname: Freitas fullname: Freitas, Sônia Maria de organization: Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Brasília, Asa Norte, Brasilia 70910-900, DF, Brazil – sequence: 8 givenname: João Alexandre R G surname: Barbosa fullname: Barbosa, João Alexandre R G organization: Laboratory of Molecular Biophysics, Department of Cell Biology, Institute of Biological Sciences, Darcy Ribeiro Campus, University of Brasília, Asa Norte, Brasilia 70910-900, DF, Brazil |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/39453204$$D View this record in MEDLINE/PubMed |
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| Keywords | snake venom serine protease coagulation cascade kallikrein–kinin system Toxicofera venom evolution hemostasis-affecting toxins venom toxin platelet activation |
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| Snippet | Toxicofera reptile venoms are composed of several toxins, including serine proteases. These proteases are glycosylated enzymes that affect the prey's... Toxicofera reptile venoms are composed of several toxins, including serine proteases. These proteases are glycosylated enzymes that affect the prey’s... |
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| SubjectTerms | 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 |
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| Title | Exploring the Diversity and Function of Serine Proteases in Toxicofera Reptile Venoms: A Comprehensive Overview |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/39453204 https://www.proquest.com/docview/3120769551 https://www.proquest.com/docview/3120599953 https://pubmed.ncbi.nlm.nih.gov/PMC11511063 https://doaj.org/article/913c09007fbd4d6693eed9a5969ddf54 |
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