Final answer:
The induced fit of an enzyme is crucial for maximizing the efficiency of the enzyme's catalytic action by enabling conformational changes upon substrate binding, leading to an optimized alignment for the reaction to proceed.
Step-by-step explanation:
The induced fit of an enzyme is essential as it enhances the enzyme's ability to bind the substrate and catalyze the chemical reaction efficiently. Formerly, the lock-and-key model explained this interaction as a simple fit between the enzyme and substrate. However, scientific advancements have led to the induced-fit model, which stipulates that this interaction is more dynamic, involving a series of conformational changes that optimize the substrate's alignment with the enzyme's active site and bring the substrate to its transition state, significantly increasing the reaction's rate.
Working with the detailed three-dimensional structures of enzymes has allowed scientists to observe that upon substrate binding, there is a conformational change in both the enzyme and the substrate. This process promotes an ideal binding environment that is necessary for the reaction to occur effectively. Once the reaction is complete and the products are released, the enzyme reverts to its original structure, ready to catalyze the same reaction again.