Allosteric inhibition

Definition

Allosteric inhibition is a form of enzyme regulation where an inhibitor molecule binds to a site other than the enzyme's active site. This binding changes the enzyme's shape, reducing its activity.

5 Must Know Facts For Your Next Test

1. Allosteric inhibitors bind to allosteric sites, not the active site.
2. Binding of an allosteric inhibitor induces a conformational change in the enzyme.
3. Allosteric inhibition can be reversible or irreversible.
4. This type of inhibition is crucial for regulating metabolic pathways.
5. Allosteric sites are distinct from the active site and have specific regulatory roles.

Review Questions

• What is the primary difference between allosteric inhibition and competitive inhibition?
• How does the binding of an allosteric inhibitor affect enzyme activity?
• Why is allosteric inhibition important for metabolic regulation?

Related terms

Active Site: The region on an enzyme where substrate molecules bind and undergo a chemical reaction

Competitive Inhibition: A form of enzyme inhibition where an inhibitor competes with the substrate for binding at the active site

Conformational Change: An alteration in the shape of a protein that can result from ligand binding or environmental changes