Probing the mechanism of purine nucleoside phosphorylase by steady-state kinetic studies and ligand binding characterization determined by fluorimetric titrations.

@article{WielgusKutrowska2006ProbingTM,
  title={Probing the mechanism of purine nucleoside phosphorylase by steady-state kinetic studies and ligand binding characterization determined by fluorimetric titrations.},
  author={Beata Wielgus-Kutrowska and Agnieszka Bzowska},
  journal={Biochimica et biophysica acta},
  year={2006},
  volume={1764 5},
  pages={887-902}
}
Reversible reaction catalyzed by trimeric purine nucleoside phosphorylase (PNP) from Cellulomonas sp. with typical and non-typical substrates, including product inhibition patterns of both reaction directions, and interactions of the enzyme with bisubstrate analogue inhibitors, were investigated by the steady-state kinetic methods and fluorimetric titrations. The ligand chromophores exist most probably as neutral species, and not N(1)-H monoanions, in the complex with PNP, as shown by… CONTINUE READING
3 Citations
0 References
Similar Papers

Similar Papers

Loading similar papers…