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. But in uncompetitive, the inhibitor can only bind to our site on that enzyme when the substrate actually binds to our active site. In fact, in uncompetitive inhibition, when the substrate, shown in blue binds to the active site of the enzyme here, when that binding takes place, only then do we create that site for this inhibitor. So we can imagine this binds, then it creates that site for our inhibitor, shown in purple, that can then bind to that site to form this enzyme substrate inhibitor complex.