Table of contents

1. Introduction to Biochemistry4h 34m
2. Water3h 23m
3. Amino Acids8h 10m
4. Protein Structure10h 4m
5. Protein Techniques14h 5m
6. Enzymes and Enzyme Kinetics13h 38m
7. Enzyme Inhibition and Regulation 8h 42m
8. Protein Function 9h 41m
9. Carbohydrates7h 49m
10. Lipids5h 49m
11. Biological Membranes and Transport 6h 37m
12. Biosignaling9h 45m
Review 1: Nucleic Acids, Lipids, & Membranes2h 47m
Review 2: Biosignaling, Glycolysis, Gluconeogenesis, & PP-Pathway3h 12m
Review 3: Pyruvate & Fatty Acid Oxidation, Citric Acid Cycle, & Glycogen Metabolism2h 26m
Review 4: Amino Acid Oxidation, Oxidative Phosphorylation, & Photophosphorylation1h 48m

6. Enzymes and Enzyme Kinetics

Michaelis-Menten Assumptions

Biochemistry

6. Enzymes and Enzyme Kinetics

Michaelis-Menten Assumptions

Previous problemNext problem

Struggling with Biochemistry?

Join thousands of students who trust us to help them ace their exams!Watch the first video

Multiple Choice

Which of the following statements best describes the Michaelis-Menten constant ($K_m$)?

$K_m$ is the maximum velocity achieved by the enzyme-catalyzed reaction.

$K_m$ is the substrate concentration at which the reaction velocity is half of $V_{max}$.

$K_m$ is the concentration of enzyme required to reach $V_{max}$.

$K_m$ is the rate constant for the formation of the enzyme-substrate complex.

Previous problemNext problem

Verified step by step guidance

Step 1: Begin by understanding the concept of the Michaelis-Menten constant ($K_m$). It is a key parameter in enzyme kinetics that provides insight into the enzyme's affinity for its substrate. Specifically, $K_m$ is defined as the substrate concentration at which the reaction velocity is half of the maximum velocity ($V_{max}$).

Step 2: Analyze the options provided in the problem. The first option states that $K_m$ is the maximum velocity achieved by the enzyme-catalyzed reaction. This is incorrect because $K_m$ is not related to $V_{max}$ directly; $V_{max}$ is the maximum reaction rate, while $K_m$ is a measure of substrate concentration.

Step 3: Evaluate the second option, which states that $K_m$ is the substrate concentration at which the reaction velocity is half of $V_{max}$. This aligns with the definition of $K_m$ in enzyme kinetics and is the correct description.

Step 4: Consider the third option, which claims that $K_m$ is the concentration of enzyme required to reach $V_{max}$. This is incorrect because $K_m$ is related to substrate concentration, not enzyme concentration.

Step 5: Review the fourth option, which suggests that $K_m$ is the rate constant for the formation of the enzyme-substrate complex. This is also incorrect because $K_m$ is not a rate constant; it is a substrate concentration value that reflects the enzyme's affinity for its substrate.