Use the relationships revealed by a Lineweaver–Burk plot and the table of enzyme performance to calculate the Vmax and KM of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B. 1/Vo Slope = Km/Vmax Intercept = -1/KM Intercept = 1/Vmax 1/[S] % (µmol/min); with no V (µmol/min); with Vo (µmol/min); with [S] (µM) inhibitor inhibitor A inhibitor B 3 10.4 4.1 2.1 14.5 6.4 2.9 10 22.5 11.3 4.5 30 33.8 22.6 6.8 90 40.5 33.8 8.1 Substrate concentration, [S], has units of micromolar, µM. Enzyme velocity, Vo, has units of micromole per minute, (µmol/min).
Use the relationships revealed by a Lineweaver–Burk plot and the table of enzyme performance to calculate the Vmax and KM of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B. 1/Vo Slope = Km/Vmax Intercept = -1/KM Intercept = 1/Vmax 1/[S] % (µmol/min); with no V (µmol/min); with Vo (µmol/min); with [S] (µM) inhibitor inhibitor A inhibitor B 3 10.4 4.1 2.1 14.5 6.4 2.9 10 22.5 11.3 4.5 30 33.8 22.6 6.8 90 40.5 33.8 8.1 Substrate concentration, [S], has units of micromolar, µM. Enzyme velocity, Vo, has units of micromole per minute, (µmol/min).
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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Question
Use the relationships revealed by a Lineweaver–Burk plot and the table of enzyme performance to calculate the ?max and ?M of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B.
Substrate concentration, [S], has units of micromolar, μM.
Enzyme velocity, ?0, has units of micromole per minute, (μmol/min).
Using data from only the extremes of the [S] range is unreliable.
Select the type of inhibition displayed by inhibitor A.
- competitive
- noncompetitive
- uncompetitive
Select the type of inhibition displayed by inhibitor B.
- competitive
- noncompetitive
- uncompetitive

Transcribed Image Text:Vmax; no inhibitor =
µmol/min
KM: no inhibitor =
µM
umol/min
KM: with inhibitor A
uM
max; with inhibitor A
umol/min
KM: with inhibitor B
uM
max; with inhibitor B
Select the type of inhibition displayed by inhibitor A.
Select the type of inhibition displayed by inhibitor B.
O competitive
competitive
noncompetitive
noncompetitive
uncompetitive
uncompetitive
![Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and KM of
the enzyme with no inhibitor, with inhibitor A, and with inhibitor B.
1/Vo Slope = KM/Vmax
%3D
Intercept = -1/KM
Intercept = 1/Vmax
1/[S]
Vo (umol/min); with no Vo (umol/min); with
Vo (µmol/min); with
IS] (µM)
inhibitor
inhibitor A
inhibitor B
3
10.4
4.1
2.1
5
14.5
6.4
2.9
10
22.5
11.3
4.5
30
33.8
22.6
6.8
90
40.5
33.8
8.1
Substrate concentration, [S], has units of micromolar, µM.
Enzyme velocity, Vo, has units of micromole per minute, (µmol/min).
Using data from only the extremes of the [S] range is unreliable.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fa061449e-1e75-4fa5-9e02-82a00bd019ab%2F71b1aef3-a6b6-46de-a851-e13b16b6beee%2Fhd35eb99_processed.png&w=3840&q=75)
Transcribed Image Text:Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and KM of
the enzyme with no inhibitor, with inhibitor A, and with inhibitor B.
1/Vo Slope = KM/Vmax
%3D
Intercept = -1/KM
Intercept = 1/Vmax
1/[S]
Vo (umol/min); with no Vo (umol/min); with
Vo (µmol/min); with
IS] (µM)
inhibitor
inhibitor A
inhibitor B
3
10.4
4.1
2.1
5
14.5
6.4
2.9
10
22.5
11.3
4.5
30
33.8
22.6
6.8
90
40.5
33.8
8.1
Substrate concentration, [S], has units of micromolar, µM.
Enzyme velocity, Vo, has units of micromole per minute, (µmol/min).
Using data from only the extremes of the [S] range is unreliable.
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