Alternative Perspectives of Enzyme Kinetic Modeling
Ryan Walsh · InTech eBooks · 2012
The basis of enzyme kinetic modelling was established during the early 1900’s when the work of Leonor Michaelis and Maud Menten produced a pseudo-steady state equation linking enzymatic catalytic rate to substrate concentration (Michaelis & Menten, 1913). Building from the Michaelis-Menten equation, other equations used to describe the effects of modifiers of enzymatic activity were developed based on their effect on the catalytic parameters of the Michaelis-Menten equation. Initially, inhibitors affecting the substrate affinity were deemed competitive and inhibitors affecting the reaction rate were labelled non-competitive (McElroy 1947). These equations have persisted as the basis for inhibition studies and can be found in most basic textbooks dealing with the subject of enzyme inhibition. Here the functionality of the competitive and non-competitive equations are examined to support the development of a unified equation for enzymatic activity modulation. From this, a modular approach to pseudo-steady state enzyme kinetic equation building is examined. Finally the assumption that these equations, which stem from the Michaelis-Menten equation, are truly pseudo-steady state is also examined.