Near attack conformers dominate β-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.

@article{Griffin2012NearAC,
  title={Near attack conformers dominate β-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.},
  author={Joanna L Griffin and Matthew W Bowler and Nicola J. Baxter and Katherine N Leigh and Hugh R W Dannatt and Andrea M. Hounslow and G Michael Blackburn and Charles Edwin Webster and Matthew J. Cliff and J. P. Waltho},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2012},
  volume={109 18},
  pages={6910-5}
}
Experimental observations of fluoromagnesate and fluoroaluminate complexes of β-phosphoglucomutase (β-PGM) have demonstrated the importance of charge balance in transition-state stabilization for phosphoryl transfer enzymes. Here, direct observations of ground-state analog complexes of β-PGM involving trifluoroberyllate establish that when the geometry and charge distribution closely match those of the substrate, the distribution of conformers in solution and in the crystal predominantly places… CONTINUE READING
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MgF3 − and α-galactose 1-phosphate in the active site of β-phosphoglucomutase form a transition state analogue of phosphoryl transfer

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