Biochemistry
Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
Bartleby Related Questions Icon

Related questions

Question
100%

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.
expand button
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.
Expert Solution
Check Mark
Knowledge Booster
Background pattern image
Recommended textbooks for you
Text book image
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Text book image
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Text book image
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Text book image
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Text book image
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Text book image
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON