We have on competitive inhibition, in which the inhibitor binds onto that allosteric side that is formed only when that substrate is bound onto the active side of the enzyme. And finally, we have noncompetitive inhibition in which that enzyme always contains an allosteric site. And so what that means is that inhibitor can bind onto that allosteric site of the enzyme regardless of whether or not that substrate is bound onto the active site of the enzyme. And finally, I guess I'll mention it briefly, we also have a fourth type of inhibition known as mixed inhibition. And in mixed inhibition, what that inhibitor does is it basically decreases the affinity of that active side for that substrate, and it also decreases the turnover number of that particular enzyme. This is known as mixed inhibition.