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2.3: Enzyme Inhibition

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    154158
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    • 2.3.1: Overview of Enzyme Regulation
      Enzymes can be slowed down or even prevented from catalyzing reactions in many ways including preventing the substrate from entering the active site or preventing the enzyme from altering conformation to catalyze the reaction. The inhibitors that do this can do so either reversibly or irreversibly. The irreversible inhibitors are also called inactivators, and reversible inhibitors are generally grouped into two basic types: competitive and non-competitive.
    • 2.3.2: Overview of Enzyme Inhibition
    • 2.3.3: Mechanisms of Enzyme Inhibition
      Enzyme inhibition reduces catalytic activity through reversible or irreversible mechanisms. Reversible inhibitors include competitive, uncompetitive, noncompetitive, and mixed inhibition. These mechanisms alter kinetic parameters such as Km and Vmax. Graphical analysis of reaction rates helps identify inhibition type.
    • 2.3.4: Protein–Ligand Binding and Affinity
      Ligand binding enables protein function through reversible noncovalent interactions. Binding affinity is described by the dissociation constant (KD). Saturation curves and binding equations illustrate how ligand concentration influences macromolecule binding. Cooperative binding and protein oligomerization affect biochemical regulation.


    2.3: Enzyme Inhibition is shared under a CC BY-SA 4.0 license and was authored, remixed, and/or curated by LibreTexts.

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