Final answer:
The active site of an enzyme lowers the activation energy needed for reactants to react, facilitating biochemical reactions without permanently altering the enzyme or requiring a higher temperature. Enzyme specificity and function are influenced by temperature and pH.
Step-by-step explanation:
The active site of an enzyme plays a crucial role in biochemical reactions because it is where the substrate molecules bind to the enzyme. This region is adept at lowering the activation energy (EA) required for a chemical reaction to occur. Contrary to creating a compartment with higher temperature, the active site provides a specific environment where substrates are brought together in an optimal orientation, thus facilitating the reaction without the need for extra energy or altering the enzyme permanently in the process.
Enzymes are specific to their substrates like puzzle pieces fitting together; this specificity is due to the unique configuration of amino acid residues in the active site. In addition to substrate binding, the active site may alter its shape during the process of catalysis, allowing the reaction to proceed along a pathway with lower EA. However, it's important to note that enzymes have an optimal temperature and pH range in which they function best, and conditions outside of this range can lead to denaturation, impairing the enzyme’s function.