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

Vmax Enzyme

Biochemistry

6. Enzymes and Enzyme Kinetics

Vmax Enzyme

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Multiple Choice

What kind of kinetics is observed initially in an enzymatic reaction under conditions where [S] is saturating?

Cooperative kinetics.

First order kinetics.

Zero order kinetics.

Second order kinetics.

The system is at equilibrium and reaction proceeds equally in both directions.

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Verified step by step guidance

Understand the concept of enzyme kinetics: Enzyme kinetics studies the rate of chemical reactions that are catalyzed by enzymes. The rate of reaction depends on the concentration of substrate [S] and the enzyme's affinity for the substrate.

Identify the condition given in the problem: The problem states that the substrate concentration [S] is saturating. This means that the enzyme active sites are fully occupied by the substrate molecules.

Recall the definition of zero-order kinetics: In zero-order kinetics, the rate of reaction is constant and independent of the concentration of the substrate. This occurs when the enzyme is saturated with substrate, and all active sites are occupied.

Relate the condition to zero-order kinetics: Since the substrate concentration is saturating, the enzyme is working at its maximum capacity, and the reaction rate is constant, which is characteristic of zero-order kinetics.

Conclude that under saturating substrate conditions, the enzymatic reaction initially exhibits zero-order kinetics, as the rate of reaction is independent of the substrate concentration.