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. 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.