Allosteric inhibition

Definition

Allosteric inhibition is a form of enzyme regulation where an inhibitor molecule binds to a site other than the active site, causing a change in the enzyme's shape. This conformational change decreases the enzyme's activity and prevents substrate binding.

5 Must Know Facts For Your Next Test

1. Allosteric inhibitors bind to allosteric sites, not active sites.
2. Binding of an allosteric inhibitor induces a conformational change in the enzyme.
3. Allosteric inhibition is reversible and can be modulated by cellular signals.
4. This mechanism is crucial for regulating metabolic pathways.
5. Allosteric inhibition can affect enzymes involved in key cellular processes like glycolysis and the Krebs cycle.

Review Questions

• What type of site does an allosteric inhibitor bind to on an enzyme?
• How does allosteric inhibition affect an enzyme's shape and function?
• Why is allosteric inhibition important for metabolic regulation?

Related terms

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

Feedback Inhibition: A regulatory mechanism whereby the end product of a metabolic pathway inhibits an upstream process or enzyme to control its own production

Enzyme Kinetics: The study of the rates at which enzymatic reactions occur and how they are affected by various conditions