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

Enzyme Kinetics

Biochemistry

6. Enzymes and Enzyme Kinetics

Enzyme Kinetics

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Multiple Choice

In enzyme kinetics, how does increasing substrate concentration generally affect the rate of product formation and enzyme activity, assuming enzyme concentration is constant?

The reaction rate increases with substrate concentration until it reaches a maximum velocity (V_{max}), after which it levels off.

The reaction rate decreases as substrate concentration increases due to enzyme inhibition.

The reaction rate remains constant regardless of substrate concentration.

The reaction rate decreases initially and then increases as substrate concentration increases.

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Verified step by step guidance

Understand the relationship between substrate concentration and enzyme activity: Enzyme kinetics is governed by the Michaelis-Menten model, which describes how the rate of product formation changes with varying substrate concentrations when enzyme concentration is constant.

Recall the concept of V_max: V_max represents the maximum velocity of the reaction when all enzyme active sites are saturated with substrate. At this point, increasing substrate concentration further will not increase the reaction rate.

Consider the initial phase of the reaction: At low substrate concentrations, the reaction rate increases proportionally with substrate concentration because more substrate molecules are available to bind to the enzyme's active sites.

Analyze the saturation effect: As substrate concentration continues to increase, the enzyme active sites become saturated, and the reaction rate approaches V_max. Beyond this point, adding more substrate does not increase the rate of product formation.

Rule out incorrect options: The reaction rate does not decrease with increasing substrate concentration unless there is enzyme inhibition. It also does not remain constant or decrease initially and then increase. The correct explanation aligns with the Michaelis-Menten model, where the rate increases until it reaches V_max.