Explain the energetic benefits of making the enzyme active site complementary to the transition state rather than to the substrate conformation. Also explain how multiple weak interactions contribute to enzyme action. (In other words, how do these weak interactions between the enzyme and the transition state lower the activation energy?)

If the enzyme active site is complementary to the substrate conformation rather than to the transition state, it is unlikely that the reaction will proceed and release a product, because the enzyme-substrate complex will be tightly bound (ΔG will raise).

On the other hand, when the enzyme active site is complementary to the transition state, the substrate will not be tightly bound and will be more prone to be transformed into the product (ΔG will be lowered) and afterward, be released.

The weak interactions (non-covalent bonds) will stabilize the energy of the transition state and reduce its energy, thus lowering the activation energy). If the transition state is stable, it will form more easily and the reaction will be more likely to proceed.