Competitive inhibition

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Comp inhib

Allosteric comp inhib 1

Michaelis-Menten plot competitive inhibition

Enzyme Inhibition lineweaver-burk plots

Competitive inhibition is a form of enzyme inhibition where a substance competes with the substrate for binding to the active site of an enzyme. In this process, the inhibitor and the substrate are both capable of binding to the enzyme, but the presence of the inhibitor prevents or reduces the amount of substrate that can bind. This type of inhibition is reversible and can be overcome by increasing the concentration of the substrate.

Mechanism

The mechanism of competitive inhibition involves the inhibitor having a similar structure to the substrate, allowing it to bind to the active site of the enzyme. However, when the inhibitor is bound, it does not undergo any reaction to form a product. This prevents the actual substrate from binding to the enzyme, reducing the rate of the reaction. The inhibitor essentially competes with the substrate for the same binding site.

Kinetics

In the presence of a competitive inhibitor, the maximum velocity (Vmax) of the enzyme reaction remains unchanged, but a higher substrate concentration (Km) is required to reach half of the Vmax. This is because the presence of the inhibitor means that more substrate is needed to outcompete the inhibitor for enzyme binding sites. The effect of competitive inhibition on enzyme kinetics can be analyzed using the Lineweaver-Burk plot, where the presence of a competitive inhibitor is indicated by an increase in the apparent Km value without affecting the Vmax.

Examples

Competitive inhibition is common in both biological systems and drug design. For example, the drug methotrexate acts as a competitive inhibitor of the enzyme dihydrofolate reductase, which is involved in the synthesis of nucleotides. By inhibiting this enzyme, methotrexate can control the rate of DNA synthesis, making it an effective treatment for certain types of cancer.

Clinical Significance

Understanding competitive inhibition is crucial in the field of pharmacology and drug design, as it provides a basis for developing drugs that can specifically target and inhibit the activity of enzymes involved in disease processes. Competitive inhibitors can be designed to have a high affinity for the active site of an enzyme of interest, offering a way to control diseases by regulating metabolic pathways.

See Also

• Enzyme kinetics
• Inhibitor (chemistry)
• Non-competitive inhibition
• Allosteric regulation

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