Now, in uncompetitive inhibition, we saw that the VMAX actually decreases, and that's because at any given time, some of those enzyme substrate complexes are going to have an inhibitor present to them, and that will decrease the number of fully functional enzymes, and so that will lower that VMAX. Now, the Kcat is not changed because the active site's ability to basically convert the substrate into the product does not change. And we said that the Km decreases because once the inhibitor binds onto that complex, it prevents that substrate from leaving that active side, and that essentially increases its affinity for the active side, increases the substrate's affinity for the active side, and decreases the Km. Now, in the case of non competitive inhibition, we said that the V max is lowered because we have less functional enzymes. And the Kcat is also lowered because once the inhibitor binds onto that enzyme, it changes the shape of that active side. It no longer makes it a perfect fit for that substrate.