How is the Activity of an Allosteric Enzyme Regulated

Question

How is the activity of an allosteric enzyme regulated?
A)By a coenzyme.
B)By covalent modification.
C)Through the binding of an effector molecule.
D)Through the binding of a competitive inhibitor.
E)By substrate binding.

Accepted Answer

Allosteric enzymes are regulated by the binding of an effector molecule, which can be an activator or an inhibitor. The binding of these molecules causes a conformational change in the enzyme, altering its activity. This type of regulation is different from competitive inhibition (D), where a molecule competes with the substrate for binding to the active site. Coenzyme (A) plays a role in enzyme catalysis, but not specifically in allosteric regulation. Covalent modification (B) can also regulate enzyme activity, but it typically involves the addition or removal of a chemical group from the enzyme, rather than binding of another molecule. Substrate binding (E) can affect enzyme activity, but it is not specific to allosteric enzymes.