Kinetic characterization of gyroxin, a serine protease from Crotalus durissus terrificus venom

• Autor(a) principal: Yonamine, Camila Miyagui [UNIFESP]
• Data de Publicação: 2012
• Outros Autores: Kondo, Marcia Yuri [UNIFESP], Juliano, Maria Aparecida [UNIFESP], Icimoto, Marcelo Yudi [UNIFESP], Baptista, Gandhi R., Yamane, Tetsuo, Oliveira, Vitor [UNIFESP], Juliano, Luiz [UNIFESP], Lapa, Antonio José [UNIFESP], Lima-Landman, Maria Teresa Riggio de [UNIFESP], Hayashi, Mirian Akemi Furuie [UNIFESP]
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Repositório Institucional da UNIFESP
• Texto Completo: http://dx.doi.org/10.1016/j.biochi.2012.07.020; http://repositorio.unifesp.br/handle/11600/35517
• topic: Gyroxin; Crotalus; Kinetic; Enzymatic; Substrate; Specificity

This work describes for the first time the characterization of the enzymatic features of gyroxin, a serine protease from Crotalus durissus terrificus venom, capable to induce barrel rotation syndrome in rodents. Measuring the hydrolysis of the substrate ZFR-MCA, the optimal pH for proteolytic cleavage of gyroxin was found to be at pH 8.4. Increases in the hydrolytic activity were observed at temperatures from 25 degrees C to 45 degrees C, and increases of NaCl concentration up to 1 M led to activity decreases. the preference of gyroxin for Arg residues at the substrate P1 position was also demonstrated. Taken together, this work describes the characterization of substrate specificity of gyroxin, as well as the effects of salt and pH on its enzymatic activity. (C) 2012 Elsevier Masson SAS. All rights reserved.