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competitive inhibition
inhibitor resembles the substrate and competes with the substrate for binding to the enzyme active site
uncompetitive inhibition
inhibitor binds directly (and only) to the ES complex, not to the free enzyme. Noncompetitive inhibitors bind to a different (allosteric) site, altering the enzyme’s shape and reducing activity regardless of substrate levels
mixed inhibition
inhibitor can bind to either free enzyme or ES, and affects the dissociation constant for S. I is a modulator of S
allosteric enzyme
a protein that changes its shape and activity when a regulatory molecule binds to a site other than the active site