Enzyme Kinetics: Michaelis-Menten Mechanism

This lecture covers the Michaelis-Menten mechanism in enzyme kinetics, explaining the transition from substrate to product through the reaction coordinate. It discusses the role of enzymes in lowering the activation energy barrier, the quasi-equilibrium state, and the impact of intrinsic properties on reaction rates. The lecture also explores the significance of ATP and ADP concentrations in cellular equilibrium and the concept of reverse reactions. Additionally, it delves into the thermodynamics of enzyme-catalyzed reactions and the energy dynamics involved in maintaining equilibrium.