3) Use the Michaelis-Menten equation to answer the following questions about the relationship between reaction velocity and substrate concentration. a) At what substrate concentration would an enzyme with a Keat of 30.0 s¹ and a KM of 0.0050 M operate at one-quarter of its maximum rate? b) Determine the fraction of Vmax that would be obtained at the following substrate concentrations: ½ KM, 2KM, 10KM c) An enzyme that catalyzes the reaction X + Y is isolated from two bacterial species. The enzymes have the same Vmax but different KM values. Enzyme A has a KM of 2 μM, and Enzyme B has a KM of 0.5 μM. The plot shows the kinetics of reactions carried out with the same concentration E of each enzyme and with [X] 1 μM. Which curve corresponds to which enzyme? Time
3) Use the Michaelis-Menten equation to answer the following questions about the relationship between reaction velocity and substrate concentration. a) At what substrate concentration would an enzyme with a Keat of 30.0 s¹ and a KM of 0.0050 M operate at one-quarter of its maximum rate? b) Determine the fraction of Vmax that would be obtained at the following substrate concentrations: ½ KM, 2KM, 10KM c) An enzyme that catalyzes the reaction X + Y is isolated from two bacterial species. The enzymes have the same Vmax but different KM values. Enzyme A has a KM of 2 μM, and Enzyme B has a KM of 0.5 μM. The plot shows the kinetics of reactions carried out with the same concentration E of each enzyme and with [X] 1 μM. Which curve corresponds to which enzyme? Time
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
Please do question 3) and explain
![3) Use the Michaelis-Menten equation to answer the following questions about the relationship between
reaction velocity and substrate concentration.
a) At what substrate concentration would an enzyme with a Keat of 30.0 s¹ and a KM of 0.0050 M
operate at one-quarter of its maximum rate?
b) Determine the fraction of Vmax that would be obtained at the following substrate concentrations:
½ KM, 2KM, 10KM
c) An enzyme that catalyzes the reaction X + Y is
isolated from two bacterial species. The enzymes
have the same Vmax but different KM values.
Enzyme A has a KM of 2 μM, and Enzyme B has a
KM of 0.5 μM. The plot shows the kinetics of
reactions carried out with the same concentration E
of each enzyme and with [X] 1 μM. Which curve
corresponds to which enzyme?
Time](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fe0719576-6288-4966-bcac-ea0ff9b5df4d%2F20463d54-8288-469f-8088-f710ab9312a4%2F0151ijg_processed.jpeg&w=3840&q=75)
Transcribed Image Text:3) Use the Michaelis-Menten equation to answer the following questions about the relationship between
reaction velocity and substrate concentration.
a) At what substrate concentration would an enzyme with a Keat of 30.0 s¹ and a KM of 0.0050 M
operate at one-quarter of its maximum rate?
b) Determine the fraction of Vmax that would be obtained at the following substrate concentrations:
½ KM, 2KM, 10KM
c) An enzyme that catalyzes the reaction X + Y is
isolated from two bacterial species. The enzymes
have the same Vmax but different KM values.
Enzyme A has a KM of 2 μM, and Enzyme B has a
KM of 0.5 μM. The plot shows the kinetics of
reactions carried out with the same concentration E
of each enzyme and with [X] 1 μM. Which curve
corresponds to which enzyme?
Time
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