Chapter 6 – Enzymatic Kinetics

Basic kinetics schemes for enzymes catalyzed reactions, such as mono- and bisubstrate cases are considered. Michaelis-Menten and Henri equations are derived and analyzed including various linearization methods. Kinetic models for cooperative enzymes are presented. Various types of enzyme inhibition and influence of pH are described. Single-molecule enzymatic kinetics based on the stochastic approach is discussed. Enantioselectivity issues are addressed for enzyme-catalyzed reactions. Generalized rate laws (convenience kinetics and modular rate laws) are illustrated in connection of enzymatic reactions. Means of enzymes immobilization are given.