The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity.

@article{Rigden1999TheSO,
  title={The structure of pyruvate kinase from Leishmania mexicana reveals details of the allosteric transition and unusual effector specificity.},
  author={Daniel J. Rigden and Simon E V Phillips and Paul A. M. Michels and Linda A Fothergill-Gilmore},
  journal={Journal of molecular biology},
  year={1999},
  volume={291 3},
  pages={615-35}
}
Glycolysis occupies a central role in cellular metabolism, and is of particular importance for the catabolic production of ATP in protozoan parasites such as Leishmania and Trypanosoma. In these organisms pyruvate kinase plays a key regulatory role, and is unique in responding to fructose 2,6-bisphosphate as allosteric activator. The determination of the first eukaryotic pyruvate kinase crystal structure in the T-state is reported. A comparison of the leishmania and yeast R-state enzymes… CONTINUE READING

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