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

Refer again to the Michaelis-Menten plot of reaction velocity ($v$) versus substrate concentration ($[S]$). In which region is the enzyme saturated with substrate?

At high $[S]$, where the curve plateaus near $V_{max}$

At low $[S]$, where the curve rises steeply from the origin

At the inflection point, where $[S] = K_m$

At zero substrate concentration

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Verified step by step guidance

Step 1: Understand the Michaelis-Menten plot. This plot represents the relationship between reaction velocity (v) and substrate concentration ([S]). The curve typically starts at the origin, rises steeply, and then plateaus as substrate concentration increases.

Step 2: Recall the concept of enzyme saturation. Enzyme saturation occurs when all active sites of the enzyme molecules are occupied by substrate molecules, meaning the enzyme is working at its maximum capacity (Vmax).

Step 3: Analyze the regions of the plot. At low [S], the curve rises steeply because the enzyme has many available active sites, and the reaction velocity increases proportionally with substrate concentration. At high [S], the curve plateaus because the enzyme becomes saturated, and adding more substrate does not increase the reaction velocity further.

Step 4: Consider the inflection point where [S] = Km. Km is the substrate concentration at which the reaction velocity is half of Vmax. This point is significant for understanding enzyme efficiency but does not indicate saturation.

Step 5: Evaluate the given options. The enzyme is saturated with substrate at high [S], where the curve plateaus near Vmax. This is the region where the enzyme cannot process additional substrate molecules faster, as all active sites are occupied.