The Fundamental Problem With Enzyme Inhibition Theory

The failure of modern enzyme inhibition drug theory stems from the derivation of the inhibition equations. These equations do not recognize the difference between the chemical equilibrium, that defines the formation of the enzyme-inhibitor complex, and the effect an inhibitor has when it binds to the enzyme. Chemical equilibriums can only be used to determine the concentration of components found in a sample, but the traditional inhibition equations define inhibition with the enzyme-inhibitor binding equilibrium, destroying their usefulness in characterizing inhibition. This problem stems from the form the inhibition term takes in these equations. The traditional Inhibition term, when it was derived, was left in an arrangement that obscures its only function as a chemical equilibrium term. However, rearranging the inhibition term to establish its link to common binding curves allows us to analyse how this inhibition term affects the classic inhibition equations, pointing the way to correcting and simplifying the modeling of drug interactions. Here we will look at the derivations of biological binding curves and enzyme inhibition equations noting the forms chemical equilibrium terms take in biological equations. This will demonstrate the traditional inhibition term is just an inverted binding curve and thus a chemical equilibrium, which provides no information about the effect produced by the formation of the enzyme-inhibitor complex. From this analysis we will look at the simple alternative for these inhibition equations that clearly distinguishes between the chemical equilibrium and the effect inhibitor binding produces resulting in a single equation that defines inhibition and activation.