Structures of mannose-6-phosphate isomerase from Salmonella typhimurium bound to metal atoms and substrate: implications for catalytic mechanism.

@article{Sagurthi2009StructuresOM,
  title={Structures of mannose-6-phosphate isomerase from Salmonella typhimurium bound to metal atoms and substrate: implications for catalytic mechanism.},
  author={Someswar Rao Sagurthi and Giri Gowda and Handanahal Subbarao Savithri and Mathur Ramabhadrashastry Narasimha Murthy},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2009},
  volume={65 Pt 7},
  pages={724-32}
}
Mannose-6-phosphate isomerase (MPI) catalyzes the interconversion of mannose 6-phosphate and fructose 6-phosphate. X-ray crystal structures of MPI from Salmonella typhimurium in the apo form (with no metal bound) and in the holo form (with bound Zn2+) and two other structures with yttrium bound at an inhibitory site and complexed with Zn2+ and fructose 6-phosphate (F6P) were determined in order to gain insights into the structure and the isomerization mechanism. Isomerization involves acid/base… CONTINUE READING

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