Substrate synergism and the steady-state kinetic reaction mechanism for EPSP synthase from Escherichia coli

Previous studies of Escherichia coli 5-enolpyruvoylshikimate-3-phosphate synthase (EPSPS, EC 2.5-1.19) have suggested that the kinetic reaction mechanism for this enzyme in the forward direction is equilibrium ordered with shilimate 3-phosphate (S3P) binding first followed by phosphoenolpyruvate (PEP). Recent results from this laboratory, however, measuring direct binding of PEP and PEP analogues to free EPSPS suggest more random character to the enzyme