So we see that in this particular equation, if we have the inhibitor bound onto that enzyme, the substrate is just as likely to bind onto that enzyme as it is to bind onto that enzyme in the absence of that inhibitor. So this reaction takes place just as likely as this reaction takes place. And because of that, the affinity of that particular substrate for the active side does not change. And so Km remains the same. So Michael is constant, describes the ability of the substrate to bind to the active side. And notice that the substrate can bind or dissociate from the active side regardless of whether or not that inhibitor is bound.