Enzyme Kinetics: Understanding Reaction Rates and Mechanisms

This lecture focuses on enzyme kinetics, detailing how enzymes catalyze reactions and the factors influencing their rates. The instructor begins by contrasting thermodynamics and kinetics, emphasizing the importance of energy barriers in reactions. The discussion includes the Michaelis-Menten equation, which describes the rate of enzyme-catalyzed reactions based on substrate concentration. Key concepts such as Vmax, Km, and catalytic efficiency (Kcat/Km) are introduced, illustrating how they characterize enzyme performance. The lecture also covers the effects of pH and temperature on enzyme activity, highlighting optimal conditions for enzymatic reactions. The instructor provides examples of various enzymes and their kinetic parameters, reinforcing the practical applications of enzyme kinetics in biological systems. The session concludes with a discussion on the limitations and assumptions of the Michaelis-Menten model, ensuring a comprehensive understanding of enzyme kinetics and its relevance in biochemistry.