Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Related questions
Question
I’m reviewing Enzyme Inhibition and am having issues wrapping my head around non-competitive and uncompetitive inhibition (and their consequent effect on Vmax / Km.)
![## Enzyme Inhibition Overview
### Graph: Enzyme Inhibition Types
**Graph Explanation:**
- The graph illustrates different types of enzyme inhibition by showing reaction velocity (V) against substrate concentration ([S]).
- **Uninhibited Reaction:** The black curve represents an uninhibited enzyme reaction, reaching a maximum velocity (Vmax). The substrate concentration at half the maximum velocity is denoted as Km.
- **Competitive Inhibition (Red Curve):** This curve shows an increase in Km with no change in Vmax, indicating the need for higher substrate concentration to reach the same velocity.
- **Non-Competitive Inhibition (Green Curve):** Here, Vmax is decreased while Km remains the same. This indicates that the inhibitor impacts Vmax but does not affect substrate binding.
- **Uncompetitive Inhibition (Purple Curve):** Both Vmax and Km are decreased. This reflects the binding of inhibitor only after the substrate is bound.
### Types of Enzyme Inhibition
1. **Competitive Inhibition**
- **Binding Site:** Active site.
- **Effect on Vmax:** Remains the same.
- **Effect on Km:** Increases.
- **Notes:** Inhibition can be overcome by increasing substrate concentration.
2. **Non-Competitive Inhibition**
- **Binding Site:** Allosteric site.
- **Effect on Vmax:** Decreases.
- **Effect on Km:** Remains the same.
- **Notes:** Does not affect substrate binding; it turns the enzyme off.
3. **Uncompetitive Inhibition**
- **Binding Site:** Allosteric site at enzyme-substrate (E-S) complex.
- **Effect on Vmax:** Decreases.
- **Effect on Km:** Decreases.
- **Notes:** Binds after the substrate, locking E-S together and preventing product formation.
4. **Mixed Inhibition**
- **Binding Site:** Allosteric site on enzyme or E-S complex.
- **Effect on Vmax:** Decreases.
- **Effect on Km:** Variable (unknown).
### Important Concepts
- **Km and Vmax:** Key indicators used to understand enzyme activity under different inhibitory conditions.
- **Allosteric Sites:** Alternative binding sites on the enzyme that affect enzyme activity without competing with the substrate at the active site.](https://content.bartleby.com/qna-images/question/3156f54e-76f9-4d5b-8710-407aa8c3b44d/a64e825c-fcd1-4539-8f4b-7235656b4435/muz94ms_processed.jpeg)
Transcribed Image Text:## Enzyme Inhibition Overview
### Graph: Enzyme Inhibition Types
**Graph Explanation:**
- The graph illustrates different types of enzyme inhibition by showing reaction velocity (V) against substrate concentration ([S]).
- **Uninhibited Reaction:** The black curve represents an uninhibited enzyme reaction, reaching a maximum velocity (Vmax). The substrate concentration at half the maximum velocity is denoted as Km.
- **Competitive Inhibition (Red Curve):** This curve shows an increase in Km with no change in Vmax, indicating the need for higher substrate concentration to reach the same velocity.
- **Non-Competitive Inhibition (Green Curve):** Here, Vmax is decreased while Km remains the same. This indicates that the inhibitor impacts Vmax but does not affect substrate binding.
- **Uncompetitive Inhibition (Purple Curve):** Both Vmax and Km are decreased. This reflects the binding of inhibitor only after the substrate is bound.
### Types of Enzyme Inhibition
1. **Competitive Inhibition**
- **Binding Site:** Active site.
- **Effect on Vmax:** Remains the same.
- **Effect on Km:** Increases.
- **Notes:** Inhibition can be overcome by increasing substrate concentration.
2. **Non-Competitive Inhibition**
- **Binding Site:** Allosteric site.
- **Effect on Vmax:** Decreases.
- **Effect on Km:** Remains the same.
- **Notes:** Does not affect substrate binding; it turns the enzyme off.
3. **Uncompetitive Inhibition**
- **Binding Site:** Allosteric site at enzyme-substrate (E-S) complex.
- **Effect on Vmax:** Decreases.
- **Effect on Km:** Decreases.
- **Notes:** Binds after the substrate, locking E-S together and preventing product formation.
4. **Mixed Inhibition**
- **Binding Site:** Allosteric site on enzyme or E-S complex.
- **Effect on Vmax:** Decreases.
- **Effect on Km:** Variable (unknown).
### Important Concepts
- **Km and Vmax:** Key indicators used to understand enzyme activity under different inhibitory conditions.
- **Allosteric Sites:** Alternative binding sites on the enzyme that affect enzyme activity without competing with the substrate at the active site.
Expert Solution
This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
This is a popular solution
Trending nowThis is a popular solution!
Step by stepSolved in 2 steps
Knowledge Booster
Similar questions
- Using the table below can you please help me answer the following. Based on your results, what can you conclude about the effect of enzyme concentration on reaction rate? Explainarrow_forwardA potent inhibitor effectively inhibits an enzyme catalyzed reaction. What kind of a Ki value you would expect for a potent inhibitor?arrow_forwardPlease help me with finding the hypotheses that are being testing in each of the three enzyme experiments(the three tables below), and predicting the results of each of the three experiments based on the hypotheses (if/then). The laboratory experiment is enzyme activity.arrow_forward
- 5. Total cholesterol can be measure using the Friedewald eouation, What is the formula for Friedewald equation? A. LDL Cholesterol + HDL Cholesterol + Triglycerides/5 B. LDL Cholestero! + HDL Cholesterol + VLDL C. LDL Cholesterol + HDL/IDL Cholesterol + VLDL D. LDL Cholesteroi + HDL Cholestero! - VLDL E. Both A and B ANSWER: RATIO: 6. There is little that can be done to control high cholesterol. А. True B. False ANSWER: RATIO: 7. Most of the cholesterol in our diet comes from Fish I. Dairy Meat II. IV. Poultry A. I and II B. Il and III C. Il and IV D. I and IV E. All of the choices ANSWER: RATIO: LDL-cholesterol is the good cholesterol A. True B. False 8. ANSWER: RATIO: 9. High cholesterol is not seen in children. А. True B. False С. ANSWER: RATIO: 10. Saturated fat, which is solid at room temperature, can raise your cholesterol. Saturated fat is most commonly found in foods such as: A. Milk B. Cheese C. Meat D. Butter E. All of the choicesarrow_forward15) The graph at right shows the results of reaction rate vs. substrate concentration for a Michaelis-Menten type enzyme 16) Th a. True b. False* reaction rate substrate concentrationarrow_forwardIf the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?arrow_forward
arrow_back_ios
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY 
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON