Show Notes
In this episode, we explore enzyme kinetics and inhibition, key concepts for the MCAT Bio/Biochem section. We’ll cover how enzymes accelerate biological reactions by lowering activation energy and introduce two models for enzyme-substrate interaction: the lock-and-key model and the induced fit model. You'll learn how to apply the Michaelis-Menten equation, focusing on factors like Km and Vmax to understand enzyme efficiency and substrate binding. We’ll also break down the different types of enzyme inhibition—competitive, non-competitive, and uncompetitive—and their effects on enzyme activity. Finally, we discuss the six major types of enzymes and their roles in biological processes, with examples like ligases, isomerases, and hydrolases. Visit www.HealthAdmissionsIQ.com for more help with the MCAT.
Jump into the conversation: (00:00) Introduction to enzyme kinetics and inhibition (01:58) Definition of enzymes and their role (03:50) Enzyme models: lock and key vs. induced fit (06:28) Michaelis-Menten Equation (10:53) Association and dissociation constants (12:34) Kcat and catalytic efficiency (14:43) Assumptions of Michaelis-Menten (18:23) Lineweaver-Burk Plot: linearized Michaelis-Menten Equation (21:09) Enzyme inhibition: reversible vs. irreversible (22:14) Competitive inhibition: Km and Vmax (24:46) Non-competitive inhibition: Effects on Km and Vmax (27:20) Irreversible inhibition (29:13) Allosteric inhibition (31:26) Homotropic and feedback inhibition (37:40) Common biological enzymes: dehydrogenase, synthetase, and kinase (43:44) MCAT Advice of the Day
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