v (micromol/sec) 120 100 80 60 40 20 0 <--X ...... Y 20 40 [A] (micromolar) 60 Enzyme X must have 2 active sites, whereas enzyme Y has only 1. The Kd for enzyme X is 25 micromolar. 80 At low substrate concentrations, enzyme Y is more effective than enzyme X at converting substrate A into product. 100 Enzyme Y reaches Vmax faster than enzyme X. At saturating substrate concentrations, enzyme X produces more product per unit time than does enzyme Y.
v (micromol/sec) 120 100 80 60 40 20 0 <--X ...... Y 20 40 [A] (micromolar) 60 Enzyme X must have 2 active sites, whereas enzyme Y has only 1. The Kd for enzyme X is 25 micromolar. 80 At low substrate concentrations, enzyme Y is more effective than enzyme X at converting substrate A into product. 100 Enzyme Y reaches Vmax faster than enzyme X. At saturating substrate concentrations, enzyme X produces more product per unit time than does enzyme Y.
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
Related questions
Question
The 2 eynzymes are affected by a substrate. Choose all correct answers.
![### Graph Explanation
The graph displays the reaction velocity (\(v\) in micromoles per second) as a function of substrate concentration \([A]\) in micromolar for two enzymes, X and Y. The lines represent the relationship between substrate concentration and reaction rate for each enzyme.
- The solid line (\(\boldsymbol{-}\)) represents enzyme X.
- The dotted line (\(\cdots\)) represents enzyme Y.
#### Key Observations:
- Enzyme X shows a steep increase in velocity with increasing substrate concentration and eventually reaches a plateau, indicating a maximum velocity (Vmax).
- Enzyme Y initially increases more rapidly at low substrate concentrations but reaches a plateau at a lower velocity compared to enzyme X.
### Statements for Evaluation
1. **Enzyme X must have 2 active sites, whereas enzyme Y has only 1.**
2. **At low substrate concentrations, enzyme Y is more effective than enzyme X at converting substrate A into product.**
3. **The \(K_d\) for enzyme X is 25 micromolar.**
4. **At saturating substrate concentrations, enzyme X produces more product per unit time than does enzyme Y.**
5. **Enzyme Y reaches Vmax faster than enzyme X.**
These statements are based on the graphical data provided and aim to analyze the behavior and characteristics of the two enzymes in different substrate conditions.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Ffb0e1de4-5e74-4932-a3a3-de04fa86d3f2%2Fbb54ea7b-4c69-4564-a8da-7a27f3720d5b%2Fbe1l0t_processed.png&w=3840&q=75)
Transcribed Image Text:### Graph Explanation
The graph displays the reaction velocity (\(v\) in micromoles per second) as a function of substrate concentration \([A]\) in micromolar for two enzymes, X and Y. The lines represent the relationship between substrate concentration and reaction rate for each enzyme.
- The solid line (\(\boldsymbol{-}\)) represents enzyme X.
- The dotted line (\(\cdots\)) represents enzyme Y.
#### Key Observations:
- Enzyme X shows a steep increase in velocity with increasing substrate concentration and eventually reaches a plateau, indicating a maximum velocity (Vmax).
- Enzyme Y initially increases more rapidly at low substrate concentrations but reaches a plateau at a lower velocity compared to enzyme X.
### Statements for Evaluation
1. **Enzyme X must have 2 active sites, whereas enzyme Y has only 1.**
2. **At low substrate concentrations, enzyme Y is more effective than enzyme X at converting substrate A into product.**
3. **The \(K_d\) for enzyme X is 25 micromolar.**
4. **At saturating substrate concentrations, enzyme X produces more product per unit time than does enzyme Y.**
5. **Enzyme Y reaches Vmax faster than enzyme X.**
These statements are based on the graphical data provided and aim to analyze the behavior and characteristics of the two enzymes in different substrate conditions.
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