Helicobacter pylori thioredoxin is an arginase chaperone and guardian against oxidative and nitrosative stresses.

@article{McGee2006HelicobacterPT,
  title={Helicobacter pylori thioredoxin is an arginase chaperone and guardian against oxidative and nitrosative stresses.},
  author={David J. McGee and S. Sandeep Kumar and Ryan J Viator and Jeffrey R Bolland and Julio Ruiz and Domenico Spadafora and Traci L. Testerman and David J. A. Kelly and Lewis K. Pannell and Henry J. Windle},
  journal={The Journal of biological chemistry},
  year={2006},
  volume={281 6},
  pages={3290-6}
}
The gastric human pathogen Helicobacter pylori faces formidable challenges in the stomach including reactive oxygen and nitrogen intermediates. Here we demonstrate that arginase activity, which inhibits host nitric oxide production, is post-translationally stimulated by H. pylori thioredoxin (Trx) 1 but not the homologous Trx2. Trx1 has chaperone activity that renatures urea- or heat-denatured arginase back to the catalytically active state. Most reactive oxygen and nitrogen intermediates… CONTINUE READING
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