So once the inhibitor binds to our enzyme, it will slightly deform our enzyme, it will change the enzyme threedimensional structure and that will also slightly change the structure of our active side. And even though the active side can still bind our substrate, the binding is no longer optimal and the enzyme activity will decrease. So once the inhibitor binds to our allosteric side, that conforms or change our enzyme, changes the shape of the enzyme, change the shape of our active side. Now, even though the substrate can still bind to that active side to form the enzyme substrate inhibitor complex, this is no longer an active enzyme because this shape is not perfect because this substrate does not fit perfectly into our enzyme. So that means at any given time, because we're going to have the inhibitor bound to our enzyme, that means we'll have less active enzyme molecules and the VMAX will be reduced. However, the ratio basically stays the same.