BIOC 3700 Chapter Notes - Chapter 14: Uncompetitive Inhibitor, Competitive Inhibition, Menton
5 Nov 2015
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Enzyme kinetics: the michaelis menten equation, analysis of kinetic data. Slope = km/vmax assumed that k 1 k2, so that the first step of the reaction achieves equilibrium. Here ks is the dissociation constant of the first step in the enzymatic reaction: assumption of steady state: figure 14-7 illustrates the progress curves of the various participants in the pre- ceding reaction model under the physiologically common. The indicated points are the same as those in fig. Note the large effect of small errors at small. [s] (large 1/[s]) and the crowding together of points at large [s]: kcat/km is a measure of catalytic efficiency kcat . [s0] n o i t a r t n e c n o. Modification of the michaelis menten model to incor- porate a back reaction yields the following reaction scheme: The general model for competitive inhibition is given by the following reaction scheme: k 1. Ei s no reaction v .
