Transition-state analysis of nucleoside hydrolase from Crithidia fasciculata.

@article{Horenstein1991TransitionstateAO,
  title={Transition-state analysis of nucleoside hydrolase from Crithidia fasciculata.},
  author={Benjamin A. Horenstein and David William Parkin and B Estupi{\~n}{\'a}n and Vern L Schramm},
  journal={Biochemistry},
  year={1991},
  volume={30 44},
  pages={10788-95}
}
The transition state of nucleoside hydrolase from the trypanosome Crithidia fasciculata has been characterized by multiple Vmax/Km kinetic isotope effects with labeled inosine and adenosine as substrates. Nucleoside hydrolase catalyzes the hydrolysis of the N-glycosidic linkage of the commonly occurring purine and pyrimidine nucleosides, with Vmax/Km ranging over 2 orders of magnitude. The kinetic isotope effects for inosine were [1'-3H] = 1.150 +/- 0.006, [2'-3H] = 1.161 +/- 0.003, [1'-14C… CONTINUE READING
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