pH modulation of transient state kinetics of enzymes. I. Simple theoretical models.
The effect of proton concentration on pre-steady-state kinetics has been investigated theoretically for enzyme reactions involving the breaking of one substrate into two products. Even for the simple double-intermediate mechanism the approach to the steady state may exhibit a rather complex kinetics, which is pH-dependent. This process may even exhibit damped oscillations. A change of pH may completely change this transient kinetics and even suppresses the oscillatory regime. A simple method is presented which allows estimation of the values of the rate and ionization constants. This procedure allows one to distinguish the simple double-intermediate mechanism from a more complex process where the 'fast' binding of the substrate induces a 'slow' conformation change of the enzyme.
D004798:Enzymes / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008954:Models, Biological; D011487:Protein Conformation; D011522:Protons
D004798:Enzymes; D011522:Protons