Now, what this also means is, because the Km increases, the finity of that substrate for the active side decreases. And that's because now we have an inhibitor that has a higher affinity for that active side. And so we have to increase the number of substrate molecules to increase the likelihood of collision with that active side to actually displace and replace that inhibitor in the active side. Now, let's move on to uncompetitive inhibition. In this type of inhibition, the only time the inhibitor can bind onto that enzyme is when the substrate is bound to that enzyme. So we have the substrate collides and binds into the active site of the enzyme.