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EI Since competitive inhibitors have no effect on the velocity at saturating (infinite) concentrations of the substrate, the intercepts of the doublereciprocal plots (1/Vmax) at all the different inhibitor concentrations are the same The lines at different inhibitor concentrations must all intersect on the y axis at the same 1/Vmax At low concentrations of substrate ([S] Km), the enzyme is predominantly in the E form The competitive inhibitor can combine with E, so the presense of the inhibitor decreases the velocity when the substrate concentration is low At low substrate concentration ([S] Km), the velocity is just Vmax[S]/Km Since the inhibitor decreases the velocity and the velocity at low substrate concentration is proportional to Vmax/Km, the presence of the inhibitor affects the slopes of the Lineweaver-Burk plots; the slope is just the reciprocal of Vmax/Km Increasing the inhibitor concentration causes Km /Vmax to increase The characteristic pattern of competitive inhibition can then be rationalized if you simply remember that a competitive inhibitor combines only with E
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If the inhibitor combines only with ES (and not E), the inhibitor exerts its effect only at high concentrations of substrate at which there is lots of ES around This means that the substrate you re varying (S) doesn t prevent the binding of the inhibitor and that the substrate and inhibitor bind to two different forms of the enzyme (E and ES, respectively) E UNCOMPETITIVE S ES E
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At very low substrate concentration ([S] approaches zero), the enzyme is mostly present as E Since an uncompetitive inhibitor does not combine with E, the inhibitor has no effect on the velocity and no effect on Vmax/Km (the slope of the double-reciprocal plot) In this case, termed uncompetitive, the slopes of the double-reciprocal plots are independent of inhibitor concentration and only the intercepts are affected A series of parallel lines results when different inhibitor concentrations are used This type of inhibition is often observed for enzymes that catalyze the reaction between two substrates Often an inhibitor that is competitive against one of the substrates is found to give uncompetitive inhibition when the other substrate is varied The inhibitor does combine at the active site but does not prevent the binding of one of the substrates (and vice versa) NONCOMPETITIVE S ES E P I
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Noncompetitive inhibition results when the inhibitor binds to both E and ES Here, both the slopes (Km/Vmax) and intercepts (1/Vmax) exhibit an effect of the inhibitor The lines of different inhibitor concentration intersect (their slopes are different), but they do not intersect on the y axis (their intercepts are different) In many texts, the existence of uncompetitive inhibitors is ignored, and noncompetitive inhibitors are called mixed The different types of inhibitors are distinguished by their effects of Km and Vmax It is difficult to rationalize the behavior of inhibitors by discussing their effects on Km ; however, it is well suited for memorization In this terminology, noncompetitive inhibition is observed when the inhibitor changes Vmax but doesn t have an effect on Km The lines intersect at a common Km on the x axis In true noncompetitive inhibition, the inhibitor does not effect Km only if the dissociation constants of the inhibitor from the EI and ESI are the same Otherwise, the point of intersection in above or below the x axis depending on which of the two inhibition constants is bigger The term mixed inhibition is used to refer to noncompetitive inhibition in which both Km and Vmax are affected by the inhibitor This is all terribly and needlessly confusing If you re not going to be an enzymologist, the best advice is to just give up
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