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- Definition: This is a type of non-competitive inhibition where the inhibitor binds to an enzyme at a site other than the active site, causing a conformational change that reduces the enzyme’s activity.
- Example: The binding of an allosteric inhibitor to an enzyme can change the shape of the enzyme, making it less effective at catalyzing its reaction.
Uncompetitive Inhibition:
- Definition: This occurs when the inhibitor binds only to the enzyme-substrate complex, not to the free enzyme. This type of inhibition typically lowers both the apparent maximum reaction rate (Vmax) and the apparent Michaelis constant (Km).
- Example: Certain drugs that bind to the enzyme-substrate complex to inhibit enzyme activity.
Mixed Inhibition:
- Definition: This type of inhibition occurs when the inhibitor can bind to either the enzyme alone or the enzyme-substrate complex, but with differentially affects the binding to one of these bindings have differentially, it affects both Vmax and the binding affects both Vmax and substrate binding to the binding to the enzyme. Mixed Inhibition of the enzyme-substrate complex. -**. Mixed Inhibition of the enzyme alone, the enzyme-substrate complex.
- Specificity**: The enzyme, the enzyme-substrate complex interaction that can be more effectively. The enzyme, but not only to the enzyme-substrate complex.
- Specific inhibitors.
- Specific Inhibition**: