What does the lock-and-key model illustrate about enzymes?

The lock-and-key model effectively illustrates how enzymes function by demonstrating the specificity of enzyme-substrate interactions. Just as a key fits into a specific lock, substrates are able to bind to their corresponding enzymes at the active site due to their complementary shapes and chemical properties. This model emphasizes the importance of structural compatibility between an enzyme and its substrate, which is crucial for effective catalysis. When the right substrate fits into the enzyme's active site, it allows the enzyme to facilitate a biochemical reaction, lowering the activation energy required and thereby increasing the reaction rate. Overall, this model encapsulates the concept of enzyme specificity and the mechanism of action in biochemical processes, making it fundamental to understanding enzyme function in biological systems.

While the other options touch on important aspects of enzyme behavior, they do not directly address the mechanism by which enzymes interact with substrates as effectively as the lock-and-key model. For instance, reusability, energy requirements, and temperature effects are critical factors for enzyme activity, but these aspects are secondary to the primary function highlighted by the lock-and-key concept.