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Lecture 10 - Lecture 10 Enzyme inhibition kinetics Review...

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Lecture 10 Enzyme inhibition kinetics Review getting and analyzing data: Product vs time for increasing substrate concentrations Initial velocity vs substrate conc. Product V o time [S] Lineweaver-Burke: 1/ V o 1/[S] Inhibition Issue: changing the rate of enzyme activity in the cell (how?) Control synthesis, degradation Make, activate zymogen Make, remove inhibitor Reversible inhibition: different types of mechanisms distinguishable by kinetics competitive non-competitive uncompetitive Competitive inhibition Inhibitor binds to the active site, competing with substrate S4 S3 S2 S1 S I V = V max [S]/([S]+K m ) 1/V = (K m /V max )(1/[S]) + 1/ V max
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For a fixed concentration of inhibitor and increasing substrate, expect the maximum to be the same, K m to increase V o [S] Equations: E + S ES E + P K m ~ [E][S]/[ES] E + I EI K I = [E][I]/[EI] E T = [E] + [ES] + [EI] See p. 399 for derivation of Michaelis-Menten: V = V max [S]/([S] + K m (1 + [I]/K I )) Note the effect of 1+[I]/K I on K m : as [I] increases, K m, apparent = K m (1 + [I]/K I ) increases; at [I] = K I , K m, apparent doubles (reduced “affinity” for S) as [S] increases, [S] >> K m (1 + [I]/K
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