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ENZYME INHIBITION

ENZYME INHIBITION. S4. S3. Product. Increasing substrate concentration. S2. S1. Time. Review: How do we characterize enzyme functions?. The rate of an enzymatic reaction depends on the concentration of substrate.

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ENZYME INHIBITION

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  1. ENZYME INHIBITION

  2. S4 S3 Product Increasing substrate concentration S2 S1 Time Review: How do we characterize enzyme functions? The rate of an enzymatic reaction depends on the concentration of substrate. The Michaelis-Menten equation relates the initial velocity of the reaction to the concentration of substrate. V V = Vmax [S]/([S]+Km) [S]

  3. Review: How do we characterize enzyme functions? The Lineweaver-Burke and Eadie-Hofstee equations transform the Michaelis-Menten data to more accurately estimate Km and Vmax. 1/V 1/V = (Km/Vmax)(1/[S]) + 1/ Vmax 1/[S] V V/[S]

  4. 1/V 1/[S] -1/Km - 1/Km, apparent

  5. -I V +I [S]

  6. -I 1/V 1/Vmax,apparent +I 1/Vmax 1/[S]

  7. -I V +I [S]

  8. 1/V +I 1/Vmax, apparent -I 1/Vmax -1/Km,apparent -1/Km 1/[S]

  9. Summary • Enzyme activity can be inhibited by compounds that interact • with the enzyme’s active site (or with other sites that change • the enzyme’s structure). • Competitive inhibitors bind to the active site and compete • with substrate. • Non-competitive inhibitors bind to a separate site and • Inactivate the active site. • Uncompetitive inhibitors bind to an enzyme-substrate complex. • The type of competition and the enzyme-inhibitor binding • affinity can be determined from Michaelis-Menten kinetic • experiments.

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