Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.

@article{Valentini2002StructureAF,
  title={Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia.},
  author={Giovanna Valentini and Laurent Roberto Chiarelli and Riccardo Fortin and Manuela Dolzan and Alessandro Galizzi and Donald J. Abraham and Changqing Wang and Paola Bianchi and Alberto Zanella and Andrea Mattevi},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 26},
  pages={23807-14}
}
Deficiency of human erythrocyte isozyme (RPK) is, together with glucose-6-phosphate dehydrogenase deficiency, the most common cause of the nonspherocytic hemolytic anemia. To provide a molecular framework to the disease, we have solved the 2.7 A resolution crystal structure of human RPK in complex with fructose 1,6-bisphosphate, the allosteric activator, and phosphoglycolate, a substrate analogue, and we have functionally and structurally characterized eight mutants (G332S, G364D, T384M, D390N… CONTINUE READING
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