So as far as I understand in mixed inhibition I can bind to either E or ES. When I binds to E the equilibrium of the E+S --> ES reaction shifts to the left (Le Chatelier's) and Km is increased (less affinity of E for S). However, when I binds to the ES complex, E+S --> ES equilibrium shifts to the right. Therefore, Km decreases (more affinity of E for S).
My question is as follows: In mixed inhibition, how do we know whether the slope Km/Vmax is increasing or decreasing. It is obvious when Km is increasing and Vmax is decreasing (Vmax always decreases) but what happens when Km and Vmax both decrease? How are we expected to know whether the decrease in Km is large enough to offset the decrease in Vmax and result in a decreasing slope?
Also, do mixed inhibitors bind to active or allosteric sites of enzymes? Kaplan states that they bind to allosteric sites but some internet resources claim that this is not the case.
Thanks!
My question is as follows: In mixed inhibition, how do we know whether the slope Km/Vmax is increasing or decreasing. It is obvious when Km is increasing and Vmax is decreasing (Vmax always decreases) but what happens when Km and Vmax both decrease? How are we expected to know whether the decrease in Km is large enough to offset the decrease in Vmax and result in a decreasing slope?
Also, do mixed inhibitors bind to active or allosteric sites of enzymes? Kaplan states that they bind to allosteric sites but some internet resources claim that this is not the case.
Thanks!