MCAT Rates & Enzyme Kinetics (Part 2)

In this Jack Westin MCAT Podcast episode, Mike and Molly turn the intimidating world of enzyme kinetics into a step-by-step masterclass you can use on your very next practice exam.

What you’ll learn

- The real meaning of a Michaelis-Menten hyperbolic curve—and why enzyme concentration must stay fixed

- How to picture Vmax, kcat, Km, and catalytic efficiency (kcat/Km) without memorizing charts

- Rapid hacks for reading a Lineweaver-Burk plot (1/Vmax on the Y-intercept, –1/Km on the X)

- Competitive vs. uncompetitive vs. mixed vs. non-competitive inhibition—how each one shifts Vmax, Km and the double-reciprocal graph

- Mike & Molly’s test-day mnemonics (👀 “Uncompetitive Inhibitors Unify” ) that keep the rules straight under pressure

- Why all allosteric inhibitors must drop Vmax (and how the MCAT likes to hide that clue)

Whether you’re baffled by the math or tripped up by the terminology, this episode gives you a clear mental framework plus concrete MCAT angles—no more hand-waving.

Want to learn more? Shoot us a text at 415-855-4435 or email us at podcast@jackwestin.com! 📱

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