True or False: Enzymes exhibit high specificity for their substrates.

Enzymes indeed exhibit high specificity for their substrates, which means they typically catalyze reactions for very particular molecules rather than a broad range of substances. This specificity is crucial for maintaining the efficiency and order of biochemical pathways within living organisms. It arises from the unique structure of the enzyme's active site, where the substrate binds. The active site has a specific shape and chemical environment that complements only certain substrate molecules, allowing for precise binding and catalysis.

This high level of specificity ensures that enzymes facilitate the correct reactions necessary for cellular function, avoiding unwanted side reactions that could disrupt metabolic processes. For example, an enzyme that catalyzes the breakdown of glucose will not effectively catalyze reactions involving other sugars, due to the differences in molecular structure. This specificity is often described using the "lock and key" model or the "induced fit" model, which both highlight how substrates fit into the enzyme’s active site uniquely.

While other factors such as environmental conditions can influence enzymatic activity (like pH or temperature), they do not fundamentally alter the specific interactions between an enzyme and its substrates. Thus, the assertion of high specificity for substrates is well-founded in the principles of enzymology.