And so they do not actually compete for the active site with that substrate. And so these non competitive inhibitors can bind to the enzyme regardless of whether or not the substrate is actually bound into the active site region. And this is shown in the following diagram. So we have the enzyme, this is the active side, this is our allosteric site to which the red inhibitor can actually bind to. So once we have this enzyme, if we have the substrate in close proximity, and this is far away, the substrate will bind until the active side to basically form this particular enzyme substrate mixture and then the enzyme substrate complex. If no inhibitors bound onto that allosteric side, this can basically catalyze the transformation of that substrate, the green molecule, into the product and by the way, forgot to throw a product.