And that's exactly why the K cat is lowered in the case in the presence of a noncompetitive inhibitor. And finally, what about the Km value? And this is and this is perhaps the difficult part of understanding how this actually affects that enzyme kinetic. So why does the Km remained constant? So the Km, in the presence of a non competitive inhibitor, remains constant. How can this remain constant, and yet the VMAX is lowered?