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
- Allosteric inhibitors bind to allosteric sites, not active sites.
- Binding of an allosteric inhibitor induces a conformational change in the enzyme.
- Allosteric inhibition is reversible and can be modulated by cellular signals.
- This mechanism is crucial for regulating metabolic pathways.
- 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?
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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
