Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt.

@article{Cho2008DephosphorylationO2,
  title={Dephosphorylation of 2,3-bisphosphoglycerate by MIPP expands the regulatory capacity of the Rapoport-Luebering glycolytic shunt.},
  author={Jaiesoon Cho and Jason S. King and Xun Qian and Adrian J Harwood and Stephen B Shears},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2008},
  volume={105 16},
  pages={5998-6003}
}
The Rapoport-Luebering glycolytic bypass comprises evolutionarily conserved reactions that generate and dephosphorylate 2,3-bisphosphoglycerate (2,3-BPG). For >30 years, these reactions have been considered the responsibility of a single enzyme, the 2,3-BPG synthase/2-phosphatase (BPGM). Here, we show that Dictyostelium, birds, and mammals contain an additional 2,3-BPG phosphatase that, unlike BPGM, removes the 3-phosphate. This discovery reveals that the glycolytic pathway can bypass the… CONTINUE READING
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