Molecular Electrostatic Potential Analysis for Enzymatic Substrates , Competitive Inhibitors , and Transition-State Inhibitors

@inproceedings{Bagdassarian1997MolecularEP,
  title={Molecular Electrostatic Potential Analysis for Enzymatic Substrates , Competitive Inhibitors , and Transition-State Inhibitors},
  author={Carey K. Bagdassarian and Vern L Schramm and Steven D Schwartz},
  year={1997}
}
Recent advances in the application of kinetic isotope effects to enzyme-catalyzed reactions have provided reliable information for enzymatic transition state structures. A method is presented for quantifying the similarity of substrates and inhibitors with their enzyme-stabilized transition states. On the basis of transition-state stabilization theory for enzymatic reactions, molecules most similar to the transition state structure bind with greatest affinity. Molecular similarity measures are… CONTINUE READING