Final answer:
The induced-fit model indeed involves a conformational change in the shape of the enzyme, which is true. The model explains that enzymes and substrates undergo changes upon binding to enhance catalysis and that the enzyme's active site is flexible, adapting to the substrate's shape.
Step-by-step explanation:
The statement that the induced-fit model involves a conformational change in the shape of the enzyme is true. This model suggests that when an enzyme binds to its substrate, both the enzyme and the substrate undergo dynamic conformational changes. As part of this process, the active site of the enzyme adapts to the shape of the substrate, which can improve the orientation for the reaction to occur efficiently.
According to the induced-fit model, when a substrate approaches an enzyme, it binds to the enzyme's active site resulting in an enzyme-substrate complex. It is during this stage that significant changes occur internally, allowing the substrates to interact effectively. For example, the enzyme may contort the substrate into its transition state, which significantly increases the reaction rate. After the reaction has taken place and the products are formed, they are released, and the enzyme reverts back to its original form, ready to catalyze another reaction.
This flexibility accounted for by the induced-fit model is essential for enzyme function and is supported by experimental observations. The binding of the substrate not only changes the enzyme's active site but also can strain and distort both the enzyme's own structure and that of the substrate, facilitating catalysis.