The conserved serine-tyrosine dipeptide in Leishmania donovani hypoxanthine-guanine phosphoribosyltransferase is essential for catalytic activity.

@article{Jardim1997TheCS,
  title={The conserved serine-tyrosine dipeptide in Leishmania donovani hypoxanthine-guanine phosphoribosyltransferase is essential for catalytic activity.},
  author={Armando Jardim and Buddy Ullman},
  journal={The Journal of biological chemistry},
  year={1997},
  volume={272 14},
  pages={
          8967-73
        }
}
Crystal structures of hypoxanthine-guanine phosphoribosyltransferase (HGPRT) proteins have implied that the translocation of a flexible loop containing a highly conserved Ser-Tyr dipeptide is necessary for the protection of the proposed oxocarbonium ion transition state of the enzyme (Eads, J. C., Scapin, G. T., Xu, Y., Grubmeyer. C., and Sacchettini, J. C. (1994) Cell 78, 325-334; Schumacher, M. A., Carter, D., Roos, D. S., Ullman, B., and Brennan, R. G. (1996) Nature Struct. Biol. 3, 881-887… CONTINUE READING

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