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

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Multiple Choice

Which step in an enzyme-catalyzed reaction was assumed to be negligible by Michaelis and Menten in their original model?

The dissociation of the enzyme-substrate complex back to enzyme and substrate ($ES \rightarrow E + S$)

The formation of the enzyme-substrate complex ($E + S \rightarrow ES$)

The binding of the enzyme to the product ($E + P \rightarrow EP$)

The reverse reaction from product back to enzyme-substrate complex ($P \rightarrow ES$)

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Verified step by step guidance

Step 1: Begin by understanding the Michaelis-Menten model, which describes the kinetics of enzyme-catalyzed reactions. This model assumes a steady-state condition where the concentration of the enzyme-substrate complex remains constant over time.

Step 2: Recall that the Michaelis-Menten model simplifies the reaction mechanism by focusing on the formation and breakdown of the enzyme-substrate complex ($E + S \rightarrow ES \rightarrow E + P$). It assumes certain steps are negligible to simplify the mathematical derivation.

Step 3: Analyze the reaction steps provided in the problem. The reverse reaction from product back to enzyme-substrate complex ($P \rightarrow ES$) is assumed negligible in the original Michaelis-Menten model. This assumption allows the model to focus on the forward reaction leading to product formation.

Step 4: Understand why this assumption is made. The reverse reaction ($P \rightarrow ES$) is typically negligible because once the product is formed, it is unlikely to revert back to the enzyme-substrate complex under normal physiological conditions.

Step 5: Conclude that the Michaelis-Menten model simplifies enzyme kinetics by neglecting the reverse reaction from product back to enzyme-substrate complex ($P \rightarrow ES$), enabling a focus on the steady-state approximation and the forward reaction dynamics.