In enzyme kinetics (biochemistry), what is the primary function of an enzyme with respect to the activation energy of a chemical reaction?

Introduction / Context:
Enzymes are biological catalysts that make metabolic reactions proceed at biologically useful rates. A key way they do this is by altering the energy landscape of a reaction. Understanding exactly how enzymes influence activation energy is foundational to biochemistry, physiology, and biotechnology.

Given Data / Assumptions:

• The comparison is about a reaction with and without enzyme.
• Temperature, pH, and reactant concentrations are assumed constant.
• The overall free energy change (delta G) of a reaction is not altered by a catalyst.

Concept / Approach:
The activation energy is the energy barrier that must be overcome for reactants to reach the transition state. Enzymes stabilize the transition state and provide an alternative reaction pathway with a lower energy barrier. Lowering activation energy increases the fraction of molecules that can reach the transition state at a given temperature, thereby increasing rate.

Step-by-Step Solution:

Verification / Alternative check:
Rate enhancement by enzymes is consistent with Arrhenius-type behavior: lower Ea leads to larger rate constants at the same temperature. Empirically, enzymes can increase rates by factors of 10^6 or more without changing delta G of reaction.

Why Other Options Are Wrong:
Increase Ea: Would slow the reaction, opposite of catalytic function. Maintain constant Ea: Would not change rate. None of these: Incorrect because decreasing Ea is precisely what catalysts do.

Common Pitfalls:
Confusing activation energy with overall thermodynamics. Enzymes do not change the equilibrium position or delta G; they only change how quickly equilibrium is reached by lowering Ea.

Final Answer:
decrease the activation energy