enzymes catalyze reactions by
irreversible inhib inhibitor covalently bonds to side chains in the active site and permanently stops the enzyme from functioning
inhib bonds non covalently to active site to inhibit a substrate
competitive inhibitors compete with the natural substrate for binding sites
noncompetitive inhibitors bind to enzyme at a different site (not the active site)
allosteric reg. an effector binds enzyme at a site diff from the active one, changing the shape
feedback inhibitions (also called the end-product inhibition) the final prodicy acts as a noncompetitive inhibitor of the first enzyme, which shuts down the pathway