Well, when the inhibitor binds onto the enzyme substrate complex, what happens is once we form the enzyme substrate inhibitor complex, that inhibitor, by binding onto that complex, it prevents that substrate from actually leaving that active side. And what that means is, because that active side does not release that substrate, the affinity of that substrate for the enzyme increases. And if the affinity of that enzyme and if the affinity of the substrate for the active side of the enzyme increases, when the inhibitor binds into the complex, the Km value decreases. And that's one way that we can explain how the Km actually decreases. Another way of explaining it is in the following manner. So since the total number of functional enzymes decreases and the VMAX decreases, that means we need to add a lower concentration of that substrate to actually reach V max divided by two.