One hypothesis aimed at improving K M is that stabilization of substrate binding in the OPH active site could increase the probability of transition state formation for OP conversion. To test this hypothesis, we augmented traditional protein approaches with computational approaches. Using molecular dynamics simulations, we analyzed the wild-type (WT) OPH active site. The analysis led to identification of amino acid residues that stabilize the OPH active site. Experiments tested the molecular dynamics predictions.