An allosteric enzyme that follows the concerted mechanism (MWC model) has a T/R ratio of 300 in the absence of substrate. Suppose that a mutation reversed the ratio. Note that R is the highly active form of the enzyme and T is the less active form of the enzyme. Select all of the effects this mutation will have on the relationship between the rate of the reaction (V) and substrate concentration ([S]). The enzyme would mostly be in the T form. The plot of V versus [S] would be shaped like an S, sigmoid. The enzyme would likely follow Michaelis-Menten kinetics. The plot of V versus [S] would be shaped like a hyperbola. The enzyme would be more active. Incorrect
An allosteric enzyme that follows the concerted mechanism (MWC model) has a T/R ratio of 300 in the absence of substrate. Suppose that a mutation reversed the ratio. Note that R is the highly active form of the enzyme and T is the less active form of the enzyme. Select all of the effects this mutation will have on the relationship between the rate of the reaction (V) and substrate concentration ([S]). The enzyme would mostly be in the T form. The plot of V versus [S] would be shaped like an S, sigmoid. The enzyme would likely follow Michaelis-Menten kinetics. The plot of V versus [S] would be shaped like a hyperbola. The enzyme would be more active. Incorrect
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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Q19:
![**Title: Impact of Mutation on Allosteric Enzyme Activity (MWC Model)**
An allosteric enzyme following the concerted mechanism (MWC model) has a T/R ratio of 300 in the absence of substrate. Suppose that a mutation reversed this ratio. Note that R is the highly active form of the enzyme, and T is the less active form.
**Consider the Effects of This Mutation on the Reaction Rate and Substrate Concentration:**
1. **The enzyme would mostly be in the T form.** ✅
2. **The plot of V versus [S] would be shaped like an S, sigmoid.** ✅
3. **The enzyme would likely follow Michaelis–Menten kinetics.** ⬜
4. **The plot of V versus [S] would be shaped like a hyperbola.** ⬜
5. **The enzyme would be more active.** ✅
**Explanation of Effects:**
- A mutation that reverses the T/R ratio to favor T would predominantly keep the enzyme in the less active T form.
- The S-shaped (sigmoid) plot of V versus [S] is characteristic of allosteric enzymes indicating cooperative binding.
- Reversed T/R suggests increased enzyme activity overall.
- Incorrect selections indicate options not applicable to the observed change.
**Conclusion:**
This analysis helps illustrate the complex behaviors of allosteric enzymes and the profound impact mutations can have on enzyme kinetics and activity.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fc94cb5d1-997a-49d0-b0ef-9ec02bf0a187%2F4e0a4669-1ee7-487f-a408-0d0e1a5babce%2Ft09u83_processed.png&w=3840&q=75)
Transcribed Image Text:**Title: Impact of Mutation on Allosteric Enzyme Activity (MWC Model)**
An allosteric enzyme following the concerted mechanism (MWC model) has a T/R ratio of 300 in the absence of substrate. Suppose that a mutation reversed this ratio. Note that R is the highly active form of the enzyme, and T is the less active form.
**Consider the Effects of This Mutation on the Reaction Rate and Substrate Concentration:**
1. **The enzyme would mostly be in the T form.** ✅
2. **The plot of V versus [S] would be shaped like an S, sigmoid.** ✅
3. **The enzyme would likely follow Michaelis–Menten kinetics.** ⬜
4. **The plot of V versus [S] would be shaped like a hyperbola.** ⬜
5. **The enzyme would be more active.** ✅
**Explanation of Effects:**
- A mutation that reverses the T/R ratio to favor T would predominantly keep the enzyme in the less active T form.
- The S-shaped (sigmoid) plot of V versus [S] is characteristic of allosteric enzymes indicating cooperative binding.
- Reversed T/R suggests increased enzyme activity overall.
- Incorrect selections indicate options not applicable to the observed change.
**Conclusion:**
This analysis helps illustrate the complex behaviors of allosteric enzymes and the profound impact mutations can have on enzyme kinetics and activity.
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