Dynamic, ligand-dependent conformational change triggers reaction of ribose-1,5-bisphosphate isomerase from Thermococcus kodakarensis KOD1.

@article{Nakamura2012DynamicLC,
  title={Dynamic, ligand-dependent conformational change triggers reaction of ribose-1,5-bisphosphate isomerase from Thermococcus kodakarensis KOD1.},
  author={Akira Nakamura and Masahiro Fujihashi and Riku Aono and Takaaki Sato and Yosuke Nishiba and Shosuke Yoshida and Ayumu Yano and Haruyuki Atomi and T. Imanaka and Kunio Miki},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 25},
  pages={20784-96}
}
Ribose-1,5-bisphosphate isomerase (R15Pi) is a novel enzyme recently identified as a member of an AMP metabolic pathway in archaea. The enzyme converts d-ribose 1,5-bisphosphate into ribulose 1,5-bisphosphate, providing the substrate for archaeal ribulose-1,5-bisphosphate carboxylase/oxygenases. We here report the crystal structures of R15Pi from Thermococcus kodakarensis KOD1 (Tk-R15Pi) with and without its substrate or product. Tk-R15Pi is a hexameric enzyme formed by the trimerization of… CONTINUE READING

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