Allosteric activator

Definition

An allosteric activator is a molecule that binds to an enzyme at a site other than the active site, inducing a conformational change that enhances the enzyme's activity. This regulation mechanism is crucial for controlling metabolic pathways in microbes.

5 Must Know Facts For Your Next Test

1. Allosteric activators bind to allosteric sites, not the active site of the enzyme.
2. The binding of an allosteric activator induces a conformational change in the enzyme structure.
3. This conformational change increases the enzyme's affinity for its substrate or enhances its catalytic activity.
4. Allosteric regulation allows for fine-tuned control of metabolic pathways, responding to cellular needs.
5. Unlike competitive inhibitors, allosteric activators do not compete with substrates for the active site.

Review Questions

• Where does an allosteric activator bind on an enzyme?
• How does an allosteric activator affect an enzyme's activity?
• What is one key difference between allosteric activators and competitive inhibitors?

Related terms

Enzyme:

A biological catalyst that speeds up chemical reactions by lowering activation energy.

Active Site:

The region on an enzyme where substrate molecules bind and undergo a chemical reaction.

Competitive Inhibitor: A molecule that competes with the substrate for binding at the active site of an enzyme, reducing its activity.