Enzymes, which are biological catalysts, perform their catalytic activity by binding to specific substrate molecules and facilitating a chemical reaction. This process can be understood through several key steps.
First, the enzyme and the substrate interact at the active site of the enzyme, a specialized region that has a shape complementary to the substrate. This interaction is often described by the ‘lock and key’ or ‘induced fit’ models, where the enzyme adjusts slightly to better fit the substrate once it binds.
Once the substrate is bound to the active site, the enzyme lowers the activation energy required for the reaction to occur. This can happen through various mechanisms, such as stabilizing transition states, bringing substrates into close proximity and proper orientation, or even providing an optimal chemical environment.
After the reaction occurs, the products formed have a different shape than the original substrate, allowing them to be released from the enzyme’s active site. The enzyme itself remains unchanged and can catalyze further reactions with new substrate molecules.
In summary, an enzyme performs catalytic activity by binding to a substrate, lowering the activation energy of a reaction, and subsequently releasing the product, thereby allowing for a continuous cycle of reaction and regeneration.