What can be done to slow down an enzyme-catalyzed reaction?

Slowing down an enzyme-catalyzed reaction can effectively be achieved by decreasing the temperature of the incubator below the enzyme's optimal temperature. Enzymes have specific temperature ranges within which they function best, often referred to as their optimal temperature. At lower temperatures, molecular motion decreases, which leads to fewer collisions between the enzyme and substrate, reducing the reaction rate. This reduction in kinetic energy impacts the ability of substrates to bind to the enzyme and can slow down the reaction significantly.

In contrast, increasing the temperature above the optimal level can initially increase the reaction rate due to higher molecular motion. However, excessive heat can lead to denaturation of the enzyme, altering its structure and rendering it ineffective.

Adding more substrate or increasing the amount of enzyme present typically increases the reaction rate, as more substrate means more chances for enzyme-substrate interactions. Similarly, higher enzyme concentrations can increase reaction rates until saturation is reached.