Chapter 8 - Energy, Enzymes, and Metabolism - 8.5 Enzyme Activities Can Be Regulated - 8.5 Recap - Learning Outcomes - Page 169: 1

An irreversible inhibitor, commonly associated with poisons, deactivates an enzyme by covalently bonding to the active site. This bond is strong enough to prevent the inhibition from being reversed by the addition of more substrate. A reversible inhibitor deactivates an enzyme through non-covalent, thus weaker interactions. A reversible inhibitor differs from an irreversible inhibitor because it can dissociate from the enzyme. Reversible inhibitors include both competitive inhibitors and noncompetitive inhibitors.

An irreversible inhibitor, commonly associated with poisons, deactivates an enzyme by covalently bonding to the active site. This bond is strong enough to prevent the inhibition from being reversed by the addition of more substrate. A reversible inhibitor deactivates an enzyme through non-covalent, thus weaker interactions. A reversible inhibitor differs from an irreversible inhibitor because it can dissociate from the enzyme. Reversible inhibitors include both competitive inhibitors and noncompetitive inhibitors.