Purine-specific nucleoside N-ribohydrolase from Trypanosoma brucei brucei. Purification, specificity, and kinetic mechanism.

@article{Parkin1996PurinespecificNN,
  title={Purine-specific nucleoside N-ribohydrolase from Trypanosoma brucei brucei. Purification, specificity, and kinetic mechanism.},
  author={David William Parkin},
  journal={The Journal of biological chemistry},
  year={1996},
  volume={271 36},
  pages={21713-9}
}
Trypanosomes have no de novo purine biosynthesis and thus depend upon salvage pathways to obtain purines for their metabolic pathways and for the biosynthesis of nucleic acids. An inosine-adenosine-guanosine preferring nucleoside hydrolase (IAG-nucleoside hydrolase) from the African trypanosome Trypanosoma brucei brucei represents approximately 0.2% of the soluble protein in this organism. The enzyme has been purified over 400-fold to >95% homogeneity from the bloodstream form of this parasite… CONTINUE READING