So in the absence of an inhibitor, that substrate is going to collide into and bind to the active site of the enzyme, forming the functional enzyme substrate complex. And then that complex will catalyze and transform the substrate into the product, which will then dissociate and be released from that active side. Now, in the absence of an inhibitor, the curve that describes the substrate concentration to the velocity is this black curve here. And notice the black curve eventually reaches a maximum velocity. That's the point when all the active sites of all the enzymes are filled by that substrate. Now, in the presence of an inhibitor, what happens is because the inhibitor resembles that substrate, it's going to bind to that same active side.