What occurs in the "induced fit model" of enzyme activity?

In the induced fit model of enzyme activity, the concept revolves around the dynamic interaction between an enzyme and its substrate. This model suggests that the enzyme's active site is not a rigid structure but has the flexibility to change shape upon binding with the substrate. When the substrate approaches, it induces a conformational change in the enzyme, enhancing the fit between the two. This altered shape facilitates the chemical reaction by properly positioning the substrate to form the transition state, thereby lowering the activation energy required for the reaction to proceed.

This concept contrasts with other models of enzyme action, such as the lock-and-key model, where the substrate is thought to fit perfectly into a static active site. The induced fit model provides a more accurate representation of how enzymes function in biological systems, emphasizing the importance of the enzyme's adaptability for achieving optimal catalysis. Additionally, this flexibility is crucial for the specificity and efficiency of enzymatic reactions, allowing enzymes to interact with substrates in a more dynamic manner.