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Compare and contrast types of inhibition based on information given. Part 1 Complete Table by replacing double question marks (??) with one of the types inhibition indicated below and single question marks with Increase, Decrease, c No change in velocity compared with control Restrict inhibition to the following types • Change • Competitive • Non-competitive Uncompetitive None Trial Km Vmax (S) [Cofactor] V (dp/dt) Inhibition Control 1 1 1 0.5 ?? 1 Decrease Increase 1 Increase 3 ?? 1 1 ?? 1 [E;) represents total enzyme concentration Part 2 Explain why the velocity in trial 1 must be 0.5 based on Michaelis-Menten Enzyme kinetics Identify the trials that could be explained by allosteric inhibition. Explain. Identify the trials that could be explained by allosteric activation. Explain

Compare and contrast types of inhibition based on information given. Part 1 Complete Table by replacing double question marks (??) with one of the types inhibition indicated below and single question marks with Increase, Decrease, c No change in velocity compared with control Restrict inhibition to the following types • Change • Competitive • Non-competitive Uncompetitive None Trial Km Vmax (S) [Cofactor] V (dp/dt) Inhibition Control 1 1 1 0.5 ?? 1 Decrease Increase 1 Increase 3 ?? 1 1 ?? 1 [E;) represents total enzyme concentration Part 2 Explain why the velocity in trial 1 must be 0.5 based on Michaelis-Menten Enzyme kinetics Identify the trials that could be explained by allosteric inhibition. Explain. Identify the trials that could be explained by allosteric activation. Explain

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
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**Compare and Contrast Types of Inhibition Based on Information Given** ### Part 1 Complete the table by replacing double question marks (??) with one of the types of inhibition indicated below and single question marks with Increase, Decrease, or No change in velocity compared with control. Restrict inhibition to the following types: - Competitive - Non-competitive - Uncompetitive - None | Trial | Inhibition | Km | Vmax | [S] | [Cofactor] | \[ET]^1 | V (dp/dt) | |-------|-------------------|----|------|-----|------------|---------|-----------| | 1 | Control | 1 | 1 | 1 | 1 | 1 | 0.5 | | 2 | ?? | 1 | 1 | Increase | 1 | 1 | ? | | 3 | ?? | 1 | Decrease | 1 | 1 | 1 | ? | | 4 | ?? | 1 | Increase | 1 | 1 | 1 | ? | ^1[ET] represents total enzyme concentration ### Part 2 1. **Explain why the velocity in trial 1 must be 0.5 based on Michaelis-Menten Enzyme kinetics.** 2. **Identify the trials that could be explained by allosteric inhibition. Explain.** 3. **Identify the trials that could be explained by allosteric activation. Explain.** ### Explanation of Tables and Concepts In Part 1, you must determine the type of inhibition and the effects on kinetic parameters (Km and Vmax) based on the scenarios given in the table. **Types of Inhibition:** - **Competitive Inhibition:** The inhibitor competes with the substrate for the active site on the enzyme. Typically, Km increases while Vmax remains the same. - **Non-competitive Inhibition:** The inhibitor binds to an allosteric site, not the active site, which causes a decrease in Vmax while Km remains unchanged. - **Uncompetitive Inhibition:** The inhibitor only binds to the enzyme-substrate complex. Both Km and Vmax decrease. - **None:** No inhibition – serves as the control. **Michaelis-Menten Kinetics:** - **Vmax
Transcribed Image Text:**Compare and Contrast Types of Inhibition Based on Information Given** ### Part 1 Complete the table by replacing double question marks (??) with one of the types of inhibition indicated below and single question marks with Increase, Decrease, or No change in velocity compared with control. Restrict inhibition to the following types: - Competitive - Non-competitive - Uncompetitive - None | Trial | Inhibition | Km | Vmax | [S] | [Cofactor] | \[ET]^1 | V (dp/dt) | |-------|-------------------|----|------|-----|------------|---------|-----------| | 1 | Control | 1 | 1 | 1 | 1 | 1 | 0.5 | | 2 | ?? | 1 | 1 | Increase | 1 | 1 | ? | | 3 | ?? | 1 | Decrease | 1 | 1 | 1 | ? | | 4 | ?? | 1 | Increase | 1 | 1 | 1 | ? | ^1[ET] represents total enzyme concentration ### Part 2 1. **Explain why the velocity in trial 1 must be 0.5 based on Michaelis-Menten Enzyme kinetics.** 2. **Identify the trials that could be explained by allosteric inhibition. Explain.** 3. **Identify the trials that could be explained by allosteric activation. Explain.** ### Explanation of Tables and Concepts In Part 1, you must determine the type of inhibition and the effects on kinetic parameters (Km and Vmax) based on the scenarios given in the table. **Types of Inhibition:** - **Competitive Inhibition:** The inhibitor competes with the substrate for the active site on the enzyme. Typically, Km increases while Vmax remains the same. - **Non-competitive Inhibition:** The inhibitor binds to an allosteric site, not the active site, which causes a decrease in Vmax while Km remains unchanged. - **Uncompetitive Inhibition:** The inhibitor only binds to the enzyme-substrate complex. Both Km and Vmax decrease. - **None:** No inhibition – serves as the control. **Michaelis-Menten Kinetics:** - **Vmax
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