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Graphs to show the effects of Inhibitors on Enzyme Action

This article provides graphical representations to demonstrate the effects of inhibitors on the rate of enzyme action, specifically focusing on substrate concentration and different types of inhibitors (competitive and non-competitive). It explains how the rate of reaction changes when the active sites are saturated or inhibited by inhibitors.

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Graphs to show the effects of Inhibitors on Enzyme Action

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  1. 3.2 Graphs to show the effects of Inhibitors on Enzyme Action

  2. Rate of reaction 1 Substrate concentration

  3. Forward Explanation

  4. 2 Rate of reaction 1 Substrate concentration

  5. Forward Every active site is saturated. The rate of the reaction is at its highest. Close Explanation

  6. 3 2 Rate of reaction 1 Substrate concentration

  7. Forward Every active site is saturated, so there is no increase in the rate of reaction. Close Example

  8. Competitive Inhibitor Revise 3 2 Rate of reaction 1 Substrate concentration

  9. Non-competitive Inhibitor Revise 2 Rate of reaction 1 Substrate concentration

  10. Forward A competitive inhibitor binds to the enzyme’s active site, and slows down the process. Close Explanation

  11. Forward The substrate will soon find an active site. The effect of a competitive inhibitor is to slow down the process. Close Explanation

  12. Revise 2 Rate of reaction 1 Substrate concentration

  13. Forward The shape of the active site changes because the non-competitive inhibitor has bound to an allosteric site; so preventing an enzyme-substrate complex from forming. Close Explanation

  14. Forward The reaction rate cannot reach the same point because the non-competitive inhibitors have changed the shape of some of the active sites. Close Explanation

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