Biochemistry | Michaelis-Menten Equation

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In this lecture, Professor Zach Murphy breaks down the Michaelis-Menten Equation, one of the most foundational concepts in enzyme kinetics. This session provides a clear and structured explanation of how enzymes function, how their activity is quantified, and how changes in substrate concentration affect reaction velocity.

We begin by introducing the basic kinetic model of enzyme-substrate interaction and derive the Michaelis-Menten equation step-by-step. Key terms like Vmax (maximum reaction velocity), Km (Michaelis constant), and their physiological interpretations are explained in detail, along with how these values reflect enzyme efficiency and substrate affinity.

This lecture also emphasizes the shape of the Michaelis-Menten curve, highlighting its hyperbolic nature and how it differs from allosteric enzyme kinetics. We touch on clinical and pharmacological applications, including how Km and Vmax are altered by competitive, noncompetitive, and uncompetitive inhibitors.

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