An extremely efficient enzyme called "efficase" catalyzes the conversion of "A" to "B." A researcher decides to mutate the enzyme in order to try to improve its performance. Following active site mutations, a significant reduction in the value of KM and Vmax was observed. Which of the following may have occurred?
A) The affinity of the enzyme for the substrate was increased to a point which did not favor propagation (continuation) of the reaction.B) The decrease in V max was not related to the decrease in K M .C) If the reaction was first-order, the change in K M cannot have affected V max .D) The stability of E+S (E+A as written above) was increased, thereby increasing the K M .E) The reverse reaction (breakdown of EA to E+A) was favored, slowing the V max .