Catalytic Efficiency
Enzymes accelerate chemical reactions by millions-fold, making vital biochemical processes occur rapidly.
Specificity
They exhibit high specificity, recognizing and interacting precisely with specific substrates due to the unique structure of their active sites.
Saturation Kinetic
Reaction rates increase with substrate concentration until enzymes are saturated, reaching a maximum velocity (Vmax) beyond which the rate plateaus.
Environmental Sensitivity:
Enzyme activity is influenced by factors like pH, temperature, and the presence of inhibitors or activators, each enzyme having optimal conditions for maximal activity.
Reversibility
Many enzyme-catalyzed reactions are reversible, with the direction dependent on substrate and product concentrations.
Regulation
Enzyme activity can be modified through mechanisms such as allosteric regulation, covalent modification, or changes in enzyme synthesis to meet metabolic demands.
Cofactor Dependence
Many enzymes require non-protein cofactors—metal ions (e.g., Mg²⁺, Zn²⁺) or organic molecules (coenzymes)—to be active.