Final answer:
Temporary bonds formed between the amino acids in the enzyme's active site and the substrate strengthen the substrate's existing bonds, making them easier to break. Enzymes, as specific macromolecules, catalyze reactions by forming an enzyme-substrate complex, thereby lowering the required activation energy.
Step-by-step explanation:
Temporary bonds between the amino acids lining the active site and the substrate strengthen the existing bonds within the substrate molecule and allow them to be easily broken. This interaction facilitates the enzymatic reaction by lowering the reaction's activation energy and promoting its rapid progression. The binding of substrates at the enzyme's active site can compromise the bond structures, enabling them to be more easily broken, and providing optimal environmental conditions for a reaction to occur.
Enzymes are macromolecules, most often proteins, that catalyze chemical reactions with high specificity. They achieve this through the formation of an enzyme-substrate complex, which changes the shape of the enzyme to better accommodate the substrate, a concept known as the induced fit model.
Due to the precise interaction between the enzyme and its substrates, which adapts to find the best fit, the enzyme's active site provides a specific chemical environment perfectly suited for the reaction. This fine-tuned mechanism of action makes enzymes efficient and essential catalysts in biological processes.