Corpus ID: 36728388

Homogeneous uridine kinase from Ehrlich ascites tumor: substrate specificity and inhibition by bisubstrate analogs.

@article{Cheng1986HomogeneousUK,
  title={Homogeneous uridine kinase from Ehrlich ascites tumor: substrate specificity and inhibition by bisubstrate analogs.},
  author={N. Cheng and R. C. Payne and W. E. Kemp and T. Traut},
  journal={Molecular pharmacology},
  year={1986},
  volume={30 2},
  pages={
          159-63
        }
}
Uridine kinase has been purified to homogeneity from Ehrlich ascites tumor cells. For the phosphate acceptor site, the enzyme shows substrate specificity only for ribopyrimidine nucleosides and is active with various analogs that have limited structural alterations; both endocyclic and exocyclic substituents can be acceptable. Of nucleosides that have been used in the chemotherapy of cancer, 5-fluorouridine, 6-azauridine, and 3-deazauridine are good substrates, whereas arabinosylcytosine is a… Expand
9 Citations
Uridine kinase: altered enzyme with decreased affinities for uridine and CTP.
Analogs of diadenosine tetraphosphate (Ap4A).
Uridine-5'-phosphate synthase: evidence for substrate cycling involving this bifunctional protein.
  • T. Traut
  • Chemistry, Medicine
  • Archives of biochemistry and biophysics
  • 1989