Effects of Competitive Inhibitors on Enzyme Kinetics

Enzymes are biological catalysts that play a critical role in increasing the rate of biochemical reactions. They lower the activation energy (Ea) of the reactions they catalyze, which allows cells to carry out complex biochemical processes at physiological temperatures.

A recent study investigated the effects of various competitive inhibitors on a specific enzyme involved in glucose metabolism. The enzyme, hexokinase, catalyzes the phosphorylation of glucose to glucose-6-phosphate. Researchers monitored reaction rates in the presence and absence of a competitive inhibitor, which mimics the substrate glucose.

As the concentration of the competitive inhibitor increased, the rate of reaction showed a characteristic pattern. Additionally, the study looked into how both substrate and inhibitor concentration influenced the reaction velocity, measuring it using Michaelis-Menten kinetics. What effect does a competitive inhibitor have on the Km and Vmax of an enzyme-catalyzed reaction?