So competitive inhibitors increase the parent Km value. So since most of the active sites are occupied by the inhibitor, a larger amount of substrate needs to be present to actually overcome and displace that inhibitor to reach that same enzyme rate. And this means a higher amount of substrate is actually needed to reach that rate of VMAX divided by two. 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.