Biochemical and Monolayer characterization of Tunisian snake venom phospholipases
| Autor: | Zaineb Abdelkafi-Koubaa, Najeh Krayem, Houcemeddine Othman, Najet Srairi-Abid, Douja Baîram, Mohamed El Ayeb, Youssef Gargouri, Hanen Louati, Naziha Marrakchi, Imen Aissa |
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| Přispěvatelé: | Laboratoire des Venins et Biomolécules Thérapeutiques - Laboratory of Venoms and Therapeutic Biomolecules (LR11IPT08), Institut Pasteur de Tunis, Réseau International des Instituts Pasteur (RIIP)-Réseau International des Instituts Pasteur (RIIP), Université de Tunis El Manar (UTM), Université de Sfax - University of Sfax, École Nationale d'Ingénieurs de Sfax | National School of Engineers of Sfax (ENIS), This work received financial support from the Ministry of Higher Education, Scientific Research in Tunisia. |
| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Stereochemistry [SDV]Life Sciences [q-bio] MESH: Viperidae Viper Venoms Phospholipase Biochemistry Hydrophobic effect 03 medical and health sciences chemistry.chemical_compound Phospholipase A2 Structural Biology Phosphatidylcholine Monolayer Viperidae Animals MESH: Animals Molecular Biology MESH: Phospholipases A2 Phospholipids MESH: Phospholipids 030102 biochemistry & molecular biology biology MESH: Kinetics Biochemical characterization Hydrolysis Substrate (chemistry) General Medicine Cerastes cerastes biology.organism_classification Kinetics Phospholipases A2 030104 developmental biology chemistry Snake venom Biophysics biology.protein Phospholipid monolayers lipids (amino acids peptides and proteins) MESH: Viper Venoms MESH: Hydrolysis |
| Zdroj: | International Journal of Biological Macromolecules International Journal of Biological Macromolecules, Elsevier, 2016, 89, pp.640-646. ⟨10.1016/j.ijbiomac.2016.05.020⟩ |
| ISSN: | 0141-8130 |
| DOI: | 10.1016/j.ijbiomac.2016.05.020⟩ |
| Popis: | International audience; The present study investigated the kinetic and interfacial properties of two secreted phospholipases isolated from Tunisian vipers'venoms: Cerastes cerastes (CC-PLA2) and Macrovipera lebetina transmediterranea (MVL-PLA2). Results show that these enzymes have great different abilities to bind and hydrolyse phospholipids. Using egg-yolk emulsions as substrate at pH 8, we found that MVL-PLA2 has a specific activity of 1473 U/mg at 37 degrees C in presence of 1 mM CaCl2. Furthermore the interfacial kinetic and binding data indicate that MVL-PLA2 has a preference to the zwitterionic phosphatidylcholine monolayers (PC). Conversely, CC-PLA2 was found to be able to hydrolyse preferentially negatively charged head group phospholipids (PG and PS) and exhibits a specific activity 9 times more important (13 333 U/mg at 60 degrees C in presence of 3 mM CaCl2). Molecular models of both CC-PLA2 and MVL-PLA2 3D structures have been built and their electrostatic potentials surfaces have been calculated. A marked anisotropy of the overall electrostatic charge distribution leads to a significantly difference in the dipole moment intensity between the two enzymes explaining the great differences in catalytic and binding properties, which seems to be governed by the electrostatic and hydrophobic forces operative at the surface of the two phospholipases |
| Databáze: | OpenAIRE |
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