What does an allosteric activator do to an enzyme?

1. Allosteric activators bind to locations on an enzyme away from the active site. 2. Their binding induces a conformational change that increases the affinity of the enzyme's active sites for its substrates. 3. Allosteric inhibitors bind in the same manner but reduce affinity instead, which is the trap in the third option. 4. Binding at the active site itself describes competitive inhibition rather than allosteric regulation. 5. So the two allosteric options differ only in direction, and an activator must raise affinity. 6. There are therefore allosteric activators as well as allosteric inhibitors. _Source: OpenStax Biology (1st ed., CC BY 4.0), Ch 6 "Metabolism", section 6.5 Enzymes_