Max value, the maximum rate of activity of that enzyme as well as the Km value, the mechaelis constant is actually lowered in uncompetitive inhibition. Now, one major difference between uncompetitive and competitive is the fact that in this particular case, if we increase the substrate concentration, that will not actually affect affect that activity of the enzyme. So uncompetitive inhibitors cannot be overcome by increasing the concentration of the substrate. And this is also true in a final type of inhibition known as non competitive inhibition. So we saw that in competitive inhibition, that inhibitor binds onto the active side of that enzyme because of the resemblance in structure. We saw that in non competitive, the only time the inhibitor can bind onto that enzyme is when the substrate is actually bound onto the active side of that enzyme, because only then will we create that pocket of space, the allosteric side that the inhibitor can actually bind to.