Kinetic isotope effects of nucleoside hydrolase from Escherichia coli.

@article{Hunt2005KineticIE,
  title={Kinetic isotope effects of nucleoside hydrolase from Escherichia coli.},
  author={Cindy Hunt and Niloufar B. Gillani and Anthony Farone and Mansoureh Rezaei and Paul C Kline},
  journal={Biochimica et biophysica acta},
  year={2005},
  volume={1751 2},
  pages={140-9}
}
rihC is one of a group of three ribonucleoside hydrolases found in Escherichia coli (E. coli). The enzyme catalyzes the hydrolysis of selected nucleosides to ribose and the corresponding base. A family of Vmax/Km kinetic isotope effects using uridine labeled with stable isotopes, such as 2H, 13C, and 15N, were determined by liquid chromatography/mass spectrometry (LC/MS). The kinetic isotope effects were 1.012+/-0.006, 1.027+/-0.005, 1.134+/-0.007, 1.122+/-0.008, and 1.002+/-0.004 for [1'-13C… CONTINUE READING