If Vmax for a reaction is 10 μM-s1 and the KM is 0.5 µM, what is the reaction velocity when the substrate concentration is 2 µM? 2 μM 5 μM 12 μM 8 μη
If Vmax for a reaction is 10 μM-s1 and the KM is 0.5 µM, what is the reaction velocity when the substrate concentration is 2 µM? 2 μM 5 μM 12 μM 8 μη
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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![**Question:**
If \( V_{max} \) for a reaction is 10 µM·s⁻¹ and the \( K_M \) is 0.5 µM, what is the reaction velocity when the substrate concentration is 2 µM?
**Options:**
1. 2 µM
2. 5 µM
3. 12 µM
4. 8 µM
---
In enzyme kinetics, the Michaelis-Menten equation describes the rate of enzymatic reactions by relating reaction rate \( V \) to the concentration of substrate \( [S] \).
The Michaelis-Menten equation is:
\[ V = \frac{V_{max} [S]}{K_M + [S]} \]
Where:
- \( V \) is the reaction velocity.
- \( V_{max} \) is the maximum reaction velocity.
- \( [S] \) is the substrate concentration.
- \( K_M \) is the Michaelis constant, which indicates the substrate concentration at which the reaction velocity is half of \( V_{max} \).
Using the provided values \( V_{max} = 10 \) µM·s⁻¹, \( K_M = 0.5 \) µM, and \( [S] = 2 \) µM, we can calculate the reaction velocity \( V \):
\[ V = \frac{10 \text{ µM·s}⁻¹ \times 2 \text{ µM}}{0.5 \text{ µM} + 2 \text{ µM}} \]
\[ V = \frac{20 \text{ µM}²\text{s}⁻¹}{2.5 \text{ µM}} \]
\[ V = 8 \text{ µM·s}⁻¹ \]
Therefore, the correct answer is:
- 8 µM](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fc3b47743-a772-4568-83ad-b77b4d2c37c7%2F03e02019-0f21-4d51-9728-6f99fcc63bf0%2Fumwkqz_processed.jpeg&w=3840&q=75)
Transcribed Image Text:**Question:**
If \( V_{max} \) for a reaction is 10 µM·s⁻¹ and the \( K_M \) is 0.5 µM, what is the reaction velocity when the substrate concentration is 2 µM?
**Options:**
1. 2 µM
2. 5 µM
3. 12 µM
4. 8 µM
---
In enzyme kinetics, the Michaelis-Menten equation describes the rate of enzymatic reactions by relating reaction rate \( V \) to the concentration of substrate \( [S] \).
The Michaelis-Menten equation is:
\[ V = \frac{V_{max} [S]}{K_M + [S]} \]
Where:
- \( V \) is the reaction velocity.
- \( V_{max} \) is the maximum reaction velocity.
- \( [S] \) is the substrate concentration.
- \( K_M \) is the Michaelis constant, which indicates the substrate concentration at which the reaction velocity is half of \( V_{max} \).
Using the provided values \( V_{max} = 10 \) µM·s⁻¹, \( K_M = 0.5 \) µM, and \( [S] = 2 \) µM, we can calculate the reaction velocity \( V \):
\[ V = \frac{10 \text{ µM·s}⁻¹ \times 2 \text{ µM}}{0.5 \text{ µM} + 2 \text{ µM}} \]
\[ V = \frac{20 \text{ µM}²\text{s}⁻¹}{2.5 \text{ µM}} \]
\[ V = 8 \text{ µM·s}⁻¹ \]
Therefore, the correct answer is:
- 8 µM
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