And the only way that the concentration of the intermediate is not changing is if the rate of formation of this intermediate is equal to the rate of dissociation. If these two rates are equal, only then will the concentration of the intermediate be actually the same. So under steady state conditions, we see that the rate of formation of the enzyme substrate complex is equal to the rate of dissociation. Now how many reactions actually describe the rate of formation? Well, we only have one reaction that forms this enzyme substrate complex. And it's this reaction here that contains the rate constant of K one.