Question

One way in which an enzyme can lower the activation energy required for a reaction is to bind the substrate(s) and distort its structure so that the substrate more closely resembles the transition state of the reaction. This mechanism will be facilitated if the shape and chemical properties of the enzyme's active site are more complementary to the transition state than to the undistorted substrate; in other words, if the enzyme were to have a higher affinity for the transition state than for the substrate. Knowing this, your friend looked in an organic chemistry textbook to identify a stable chemical that closely resembles the transition state of a reaction that converts X into Y. She generated an antibody against this transition-state analog and mixed the antibody with chemical X. What do you think might happen?

Answer 1

When an enzyme binds its substrate, it distorts the structure to resemble the transition state, lowering the activation energy. If an antibody is generated against a transition state analog and mixed with a chemical, it can potentially lower the activation energy of the reaction.

Step-by-step explanation:

An enzyme can lower the activation energy required for a reaction by binding the substrate and distorting its structure to resemble the transition state of the reaction. This mechanism is facilitated if the enzyme's active site has a higher affinity for the transition state than for the substrate.

In the given scenario, if your friend generated an antibody against a stable chemical that closely resembles the transition state of a reaction converting X into Y and mixed it with chemical X, the antibody would bind to chemical X in a way that distorts its structure to resemble the transition state. This can potentially lower the activation energy of the reaction and facilitate the conversion of X into Y.