Final answer:
Enzymatic reactions are more useful than non-enzymatic chemical reactions because enzymes are active at physiological conditions and are highly specific catalysts that lower the activation energy of only certain chemical reactions, making biological processes efficient and controlled.
Step-by-step explanation:
The best summary as to why enzymatic reactions are sometimes more useful than non-enzymatic chemical reactions is that enzymes are active at physiological pH and temperature, and they catalyze specific reactions. This capability makes them incredibly efficient for biological processes. Unlike other catalysts that might require extreme conditions, enzymes operate optimally at conditions compatible with life, which is critical for the functioning of living organisms. Furthermore, their high specificity ensures that reactions proceed with fewer by-products and more control.
Enzymes function as nature's own catalysts, accelerating the chemical reactions necessary for life. They do this by lowering the activation energy of a reaction. Enzymes behave with extreme specificity, recognizing only particular reactants as substrates and catalyzing only certain reactions. This level of precision helps maintain the intricate balance of metabolic pathways within cells. Additionally, enzymes are able to catalyze reactions repeatedly without being consumed, making them very efficient.
Moreover, enzymes facilitate reactions in ways that align precisely with the needs of cells. For instance, their ability to bring reactants into an optimal orientation and create a conducive environment within the active site allows biochemical reactions to proceed at rates that support life processes efficiently. An example is the protease enzymes used in various products to target specific peptide bonds in proteins, indicating enzymes' specialized action.