And this simply was not true for the case of on competitive inhibition. In on competitive inhibition, once the inhibitor binds onto the enzyme substrate complex, it blocks that substrate from leaving the active side, and that increases the affinity of the substrate for the active side. And so that decreases that apparent Km value. 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.