Final answer:
Enzymes are more specific than inorganic catalysts because their active site's unique shape allows selective binding to substrates, aided by enzyme flexibility for allosteric regulation.
Step-by-step explanation:
Enzymes exhibit more specificity than inorganic catalysts because the shape and chemistry of the active site of an enzyme restricts the molecules that can bind to it. Unlike inorganic catalysts, enzymes possess highly specific structures tailored to bind particular substrates. This enhances not only their efficiency but also their effectiveness in catalyzing biochemical reactions. Enzymes are able to achieve this level of specificity due to their intricate three-dimensional conformation, which is critical to their function.
The active site's unique shape is designed to selectively bind to specific substrate molecules, leading to a reaction. Enzyme flexibility also allows for allosteric regulation, where the enzyme can change shape in response to cellular metabolites, further refining the control over reaction rates. In contrast, inorganic catalysts lack such specificity and function through weaker, less selective interactions with reactants.
Enzymes exhibit more specificity than inorganic catalysts because of the shape and chemistry of the active site of an enzyme, which restricts the molecules that can bind to it. Enzymes have evolved specific shapes with physical-chemical properties, allowing them to attract only the substrates necessary for a particular biochemical reaction. The active site of an enzyme has a high affinity for its substrate, resulting in enzymes being more efficient and faster catalysts compared to inorganic catalysts.