OMP decarboxylase: an experimental test of electrostatic destabilization of the enzyme-substrate complex.

@article{Callahan2004OMPDA,
  title={OMP decarboxylase: an experimental test of electrostatic destabilization of the enzyme-substrate complex.},
  author={Brian P Callahan and Richard Wolfenden},
  journal={Journal of the American Chemical Society},
  year={2004},
  volume={126 45},
  pages={14698-9}
}
6-Methylaminouridine 5'-phosphate (MAUMP) inhibits OMP decarboxylase (Ki = 3 x 10-6 M) maximally at pH values where its amino group is uncharged. Comparison of the chemical shift of free [7-13C]-MAUMP in solutions of varying pH, with that of the enzyme-bound species confirms that this inhibitor is bound with its amino group uncharged. This enzyme's apparent lack of affinity for a cationic substituent, located near the position that would ordinarily be occupied by the scissile carboxylate group… CONTINUE READING

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