And so that's exactly why that inhibitor will compete with the substrate for that active site. And we see in competitive inhibition that inhibitor binds onto that same active site that the substrate actually binds to. So in this inhibition, the inhibitor molecule typically resembles that substrate and can therefore bind into the active side of that enzyme. And once bound, the inhibitor prevents that substrate from actually occupying that active side. Now, what competitive inhibition does, and we'll discuss this in much more detail in the next lecture, is it keeps the V max the same, so it keeps the maximum velocity of that enzyme the same, but it increases the parent Km value, it increases the mechaless constant, and we'll see exactly what that means and why. That's the case in the next lecture.