Artículo
Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity
Arias, Diego Gustavo
; Reinoso, Anahí; Sasoni, Natalia
; Hartman, Matias Daniel
; Iglesias, Alberto Alvaro
; Guerrero, Sergio Adrian
Fecha de publicación:
09/2014
Editorial:
Elsevier
Revista:
Free Radical Biology And Medicine
ISSN:
0891-5849
Idioma:
Inglés
Tipo de recurso:
Artículo publicado
Clasificación temática:
Resumen
Little is known about the mechanisms by which Leptospira interrogans, the causative agent of<br />leptospirosis,copes with oxidative stress at the time it establishes persistent infection with in its human host. Were port the molecular cloning of a gene encoding a 2-Cys peroxiredoxin (LinAhpC) from this bacterium. After bioinformatic analysis we found that LinAhpC contains the characteristic GGIG and YF motifs present in peroxiredoxins that are sensitive to overoxidation (mainly eukaryotic proteins).These motifs are absent in insensitive prokaryotic enzymes. Recombinant LinAhpC showed activity as a thioredoxin peroxidase with sensitivity to overoxidation by H2O2 (Chyp1% 30 mM at pH 7.0and 30 °C). So far, Anabaena 2-Cysperoxiredoxin, Helicobacter pylori AhpC, and LinAhpC are the only prokaryotic enzymes studied with these characteristics.The properties determined for LinAhpC suggest that the protein could be critical for the antioxidant defense capacity in L. interrogans.
Archivos asociados
Licencia
Identificadores
Colecciones
Articulos(IAL)
Articulos de INSTITUTO DE AGROBIOTECNOLOGIA DEL LITORAL
Articulos de INSTITUTO DE AGROBIOTECNOLOGIA DEL LITORAL
Citación
Arias, Diego Gustavo; Reinoso, Anahí; Sasoni, Natalia; Hartman, Matias Daniel; Iglesias, Alberto Alvaro; et al.; Kinetic and structural characterization of a typical 2-cysteine peroxiredoxin from Leptospira interrogans exhibiting redox sensitivity; Elsevier; Free Radical Biology And Medicine; 77; 9-2014; 30-40
Compartir
Altmétricas