1 / 13

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.

rashad-herring
Download Presentation

ENZYME INHIBITION

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript

  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.

More Related