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. So that basically means that the Km, our mechanics constant, remains constant, which means that the affinity of the enzyme to the substrate will not be decreased or increased as it was in this particular case. And finally, let's move on to uncompetitive inhibition. Now, the major difference between non competitive and uncompetitive is in non competitive, this inhibitor can bind to the allosteric site regardless of whether the enzyme is bound to the substrate or not.