So this is how these three reversible inhibition processes actually affect enzyme kinetics. In the case of competitive inhibition, we see that the VMAX does not actually change because we can ultimately overcome that inhibition by increasing the concentration of S, the K Cab, the turnover number doesn't change because the efficiency of that active side, the fully functional active side, does not change. And we saw that the Km value actually is increased because we require a higher concentration to reach the rate of VMAX divided by two. 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.