In the notes we saw the Michaelis-Menten equation as the following: E+SkoffkonESkcatE+PKm=konkofl+kcat A) We mentioned that when Km is small, the enzyme has a higher affinity for its target, how does this makes sense give the equation for Km above? Again, I'm looking for a conceptual understanding of what's going on, so frame your answer in terms of the relative size of the k values in the expression above. Next, consider the graph below: Next, consider the graph below: B) As we learned in class, Km (or, as it's written here KM) is also the concentration of substrate ([S]) at which the reaction velocity (i.e. rate) is half the Vmax (the maximum rate). What would a lower Km mean in this case, in terms of the substrate? How does this make sense in light of your answer to part (A) about the binding affinity for the enzyme for its substrate? NOTE: you should not need to use any equations or do any calculations for your answer, simply explain in conceptual terms what these equations and graphs are trying to convey