Reversible Michaelis Menten kinetics enzyme kinetic modeling

The kinetics of the general enzyme-catalyzed reaction (equation 10.1-1) may be simple or complex, depending upon the enzyme and substrate concentrations, the presence/absence of inhibitors and/or cofactors, and upon temperature, shear, ionic strength, and pH. The simplest form of the rate law for enzyme reactions was proposed by Henri (1902), and a mechanism was proposed by Michaelis and Menten (1913), which was later extended by Briggs and Haldane (1925). The mechanism is usually referred to as the Michaelis-Menten mechanism or model. It is a two-step mechanism, the first step being a rapid, reversible formation of an enzyme-substrate complex, ES, followed by a slow, rate-determining decomposition step to form the product and reproduce the enzyme ... 

In this section the basic kinetic model for enzyme-catalyzed bioconversions is presented. Understanding this model is the foundation for deriving more complex models. In their theory of enzyme catalysis, Michaelis and Menten 113 postulated the existence of an enzyme substrate complex (ES), which is built up in a reversible... 

Kinetic Model Reversible CYP inhibition is dependent on the mode of interaction between CYP enzymes and inhibitors and is further characterized as competitive, noncompetitive, uncompetitive, and mixed. Evaluation of reversible inhibition of CYP reactions is often conducted under conditions where Michaelis-Menten (MM) kinetics is obeyed. Based on Scheme 1 below, various types of reversible inhibition are described from the scheme during catalysis which can lead to enzyme inhibition ... 

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