In this case, we saw that the Km value increased because we need a higher concentration of S to reach that same particular rate. But in this particular case, that substrate is just as likely to bind until the enzyme in the absence as in the presence of that inhibitor. And so the Km value does not actually change. 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.