ABSTRACT
Enzymes are marvelous in their ability to catalyze reactions. Even more impressive is their ability to be attuned, so that they do not continue catalyzing reactions beyond what is needed biologically. They can be inhibited in their activity in multiple different ways. If the concentration of the inhibitor goes very high, there is less free enzyme to bind the substrate. Commonly, though not always, competitive inhibition occurs when the inhibitor and the substrate bind to the same location on the enzyme. Some inhibitors bind only to the enzyme–substrate complex, as seen in the binding scheme depicted. Sometimes the inhibitor is capable of binding both to the free enzyme and also to the enzyme substrate complex. Acid phosphatases are a group of enzymes that non-specifically catalyze the hydrolysis of phosphate esters. Phosphate itself is a product of the reaction, and as such can bind to the free enzyme.
