Question

Which statement most accurately explains how allosteric regulation can change an enzyme's catalytic activity? View Available Hint(s) Which statement most accurately explains how allosteric regulation can change an enzyme's catalytic activity? In allosteric activation, a regulatory molecule binds to a location other than the active site, resulting in a change in enzyme shape that allows the active site to bind substrate. In allosteric activation, a regulatory molecule binds to the active site, allowing substrate binding. In allosteric inhibition, a regulatory molecule binds to the active site, blocking substrate binding. In allosteric inhibition, a regulatory molecule binds to a location other than the active site, resulting in a change in enzyme shape that allows the active site to bind substrate.

Answer 1

Answer:

In allosteric inhibition, a regulatory molecule binds to a location other than the active site, resulting in a change in enzyme shape that allows the active site to bind substrate.

Explanation:

Allosteric regulation of an enzyme can be positive or negative, but it always involves effector molecules that bind to non-active site of the enzyme and change its conformation. That site of binding is called allosteric or regulatory site. If the enzyme activity is enhanced effector molecule is called allosteric activator but if the activity is decreased effector molecules are allosteric inhibitors.