The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] U = Km + [S] where v is the velocity, or rate, Vmax is the maximum velocity, Km is the Michaelis-Menten constant, and [S] is the substrate concentration. A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (vo) at different substrate concentrations ([S]). First, move the line labeled Vmax to a position that represents the maximum velocity of the enzyme. 300 V Next, move the line labeled 1/2 Vmax to its correct position. max 275 Then, move the line labeled Km to its correct position. 250 225 200 175 Michaelis–Menten curve 150 K a 125 m 100 1/2 V 75 max 50 25 10 20 30 40 50 60 70 80 90 100 [S] (µM) Incorrect Estimate the values for Vmax and Km. Vmax 175 µM/min Km 14 µM v (µM/min)
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] U = Km + [S] where v is the velocity, or rate, Vmax is the maximum velocity, Km is the Michaelis-Menten constant, and [S] is the substrate concentration. A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (vo) at different substrate concentrations ([S]). First, move the line labeled Vmax to a position that represents the maximum velocity of the enzyme. 300 V Next, move the line labeled 1/2 Vmax to its correct position. max 275 Then, move the line labeled Km to its correct position. 250 225 200 175 Michaelis–Menten curve 150 K a 125 m 100 1/2 V 75 max 50 25 10 20 30 40 50 60 70 80 90 100 [S] (µM) Incorrect Estimate the values for Vmax and Km. Vmax 175 µM/min Km 14 µM v (µM/min)
Principles of Modern Chemistry
8th Edition
ISBN:9781305079113
Author:David W. Oxtoby, H. Pat Gillis, Laurie J. Butler
Publisher:David W. Oxtoby, H. Pat Gillis, Laurie J. Butler
Chapter18: Chemical Kinetics
Section: Chapter Questions
Problem 49P
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![The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction.
Vmax [S]
U =
Km + [S]
where v is the velocity, or rate, Vmax is the maximum velocity, Km is the Michaelis-Menten constant, and [S] is the
substrate concentration.
A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (vo) at different substrate concentrations
([S]).
First, move the line labeled Vmax to a position that represents
the maximum velocity of the enzyme.
300
V
Next, move the line labeled 1/2 Vmax to its correct position.
max
275
Then, move the line labeled Km to its correct position.
250
225
200
175
Michaelis–Menten curve
150
K
a 125
m
100
1/2 V
75
max
50
25
10
20
30
40
50
60
70
80
90
100
[S] (µM)
Incorrect
Estimate the values for Vmax and Km.
Vmax
175
µM/min
Km
14
µM
v (µM/min)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F8b43fcf2-0c31-4621-bb6f-bb4e7d883fd1%2F98534652-4bab-42b5-b9e1-91f4aa17aa8e%2Fok6co87.png&w=3840&q=75)
Transcribed Image Text:The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction.
Vmax [S]
U =
Km + [S]
where v is the velocity, or rate, Vmax is the maximum velocity, Km is the Michaelis-Menten constant, and [S] is the
substrate concentration.
A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (vo) at different substrate concentrations
([S]).
First, move the line labeled Vmax to a position that represents
the maximum velocity of the enzyme.
300
V
Next, move the line labeled 1/2 Vmax to its correct position.
max
275
Then, move the line labeled Km to its correct position.
250
225
200
175
Michaelis–Menten curve
150
K
a 125
m
100
1/2 V
75
max
50
25
10
20
30
40
50
60
70
80
90
100
[S] (µM)
Incorrect
Estimate the values for Vmax and Km.
Vmax
175
µM/min
Km
14
µM
v (µM/min)
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