Which of the following statements is true regarding enzyme specificity?

Enzymes demonstrate high specificity primarily due to the precise shape and chemical environment of their active sites. The active site is uniquely structured to match a specific substrate, much like a key fits into a lock. This geometric compatibility is critical and ensures that enzymes catalyze specific reactions rather than interacting with any molecule indiscriminately.

The specific amino acid residues within the active site not only provide a fitting structure but can also offer the necessary chemical interactions—such as hydrogen bonds, ionic interactions, and van der Waals forces—that stabilize the enzyme-substrate complex and facilitate the conversion of substrates to products. This targeted interaction allows enzymes to function effectively at their optimal rates while minimizing unintended reactions with other molecules.

The other statements do not accurately convey the nature of enzyme specificity. For instance, enzymes cannot bind any substrate, as specificity is a hallmark of enzyme function. While liquid mediums do promote enzyme activity due to favorable conditions for interactions, they do not directly influence the inherent specificity of the enzyme. Lastly, while pH can affect enzyme activity by altering the charge properties of the enzyme and substrate, it is not the sole factor determining specificity, which is primarily dictated by the structural compatibility of the active site with its substrate.