Non-competitive inhibition

Non-competitive inhibition occurs when an inhibitor binds to a different part of an enzyme (not the active site), causing a change in its shape. This structural change prevents the enzyme from functioning properly, even if the usual substrate binds to the active site. Unlike competitive inhibition, where the inhibitor directly blocks the substrate’s binding, non-competitive inhibitors reduce the enzyme’s overall activity regardless of substrate concentration. This process effectively lowers the enzyme’s ability to catalyze reactions without competing directly with the substrate, serving as a regulatory mechanism to control biological reactions.