What describes the mechanism by which an enzyme changes shape upon substrate binding, facilitating catalysis?

The induced-fit model describes the mechanism by which an enzyme undergoes a conformational change upon the binding of a substrate. In this model, the initial interaction between the enzyme and the substrate is not a perfect fit; instead, the binding of the substrate induces a change in the enzyme's structure. This alteration allows the active site to better accommodate the substrate, enhancing the ability of the enzyme to catalyze the chemical reaction.

This concept contrasts with the lock and key model, where the enzyme is seen as a rigid structure that perfectly fits the substrate, suggesting that no change occurs upon binding. Induced-fit acknowledges that the enzyme's flexibility plays a crucial role in its function, enabling the enzyme to be more efficient in lowering the activation energy required for the reaction. Moreover, active site adjustment and enzyme-substrate compatibility are not established terms that describe the mechanism of enzymatic action in the same way, making the induced-fit model the most accurate description of enzyme behavior upon substrate binding.