The steady state assumption as applied to enzyme kinetics implies

The Steady State Assumption As Applied to Enzyme Kinetics

Generally, the steady state assumption is applied to enzyme kinetics and implies that the concentration of the ES complex in the reaction mixture remains constant at all times. In enzyme catalyzed reactions, the rate of formation of the ES complex is a function of the percentage of the enzyme population that is interacting with the substrate.

The steady state assumption is used to derive the Michaelis-Menten equation, which is a closed-form solution of the enzyme kinetics for single substrate reactions. This equation is widely accepted as valid under the steady state assumption. However, it is not valid for allenzymes.

Enzyme catalyzed reactions follow the same rules as other chemical reactions. The rate of reaction is a function of the rate of reactant consumption, as well as the concentrations of substrate and product. Typically, the substrate-bound enzyme concentration changes slower than the product and substrate concentrations. The reaction rate is also determined by the inhibitor.

The steady state assumption is usually implicit in standard biochemistry textbooks. However, it is not necessary to assume s during the initial transient. The steady state assumption is valid when s is about equal to s0. In addition, the depletion of s during the initial transient must be small. This is because the enzyme-substrate complex is an intermediate.

The steady state assumption is a necessary prerequisite to the validity of the Michaelis-Menten equation. The Michaelis-Menten equation shows that the rate of a reaction is a function of the percent of the enzyme population that is interacting with its substrate.