1. Foundations

Enzyme Kinetics — Quiz

Test your understanding of enzyme kinetics with 5 practice questions.

Practice Questions

Question 1

Given enzymes X with $k_{cat}=100\\ \mathrm{s^{-1}}$ and $K_{m}=20\\ \mu\mathrm{M}$ and Y with $k_{cat}=150\\ \mathrm{s^{-1}}$ and $K_{m}=50\\ \mu\mathrm{M}$, which enzyme has the higher catalytic efficiency ($k_{cat}/K_{m}$)?

Question 2

Mixed inhibitors bind both the free enzyme and the enzyme–substrate complex with different affinities. How do mixed inhibitors generally affect the apparent $K_{m}$ and $V_{max}$?

Question 3

In a Michaelis–Menten reaction with $V_{max}=200\\ \mu\mathrm{M/min}$, $K_{m}=50\\ \mu\mathrm{M}$, and substrate concentration $[S]=25\\ \mu\mathrm{M}$, what is the initial velocity $V_{0}$?

Question 4

Which axes are used in an Eadie–Hofstee plot for enzyme kinetics?

Question 5

Which feature differentiates allosteric enzymes from classic Michaelis–Menten enzymes in their response to substrate concentration?