Substrate concentration, [S], has units of micromolar, µM. Enzyme velocity, V₁, has units of micromole per minute, (µmol/min). Using data from only the extremes of the [S] range is unreliable. Vmax; no inhibitor = Vmax; with inhibitor A = Vmax; with inhibitor B = μmol/min O noncompetitive competitive uncompetitive μmol/min μmol/min Select the type of inhibition displayed by inhibitor A. KM; no inhibitor = KM; with inhibitor A = KM; with inhibitor B = Select the type of inhibition displayed by inhibitor B. O uncompetitive competitive O noncompetitive μM μM μΜ
Substrate concentration, [S], has units of micromolar, µM. Enzyme velocity, V₁, has units of micromole per minute, (µmol/min). Using data from only the extremes of the [S] range is unreliable. Vmax; no inhibitor = Vmax; with inhibitor A = Vmax; with inhibitor B = μmol/min O noncompetitive competitive uncompetitive μmol/min μmol/min Select the type of inhibition displayed by inhibitor A. KM; no inhibitor = KM; with inhibitor A = KM; with inhibitor B = Select the type of inhibition displayed by inhibitor B. O uncompetitive competitive O noncompetitive μM μM μΜ
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
100%
Q17:
![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.
Vmax; no inhibitor =
Vmax; with inhibitor A =
Vmax; with inhibitor B =
μmol/min
O noncompetitive
O competitive
O uncompetitive
µmol/min
μmol/min
Select the type of inhibition displayed by inhibitor A.
KM; no inhibitor =
KM; with inhibitor A
=
KM; with inhibitor B =
Select the type of inhibition displayed by inhibitor B.
O uncompetitive
O competitive
Ononcompetitive
μΜ
μΜ
μM](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fc94cb5d1-997a-49d0-b0ef-9ec02bf0a187%2F13f9d616-b75d-4902-98a8-0f4cddbae0f1%2F0c983z_processed.png&w=3840&q=75)
Transcribed Image Text: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.
Vmax; no inhibitor =
Vmax; with inhibitor A =
Vmax; with inhibitor B =
μmol/min
O noncompetitive
O competitive
O uncompetitive
µmol/min
μmol/min
Select the type of inhibition displayed by inhibitor A.
KM; no inhibitor =
KM; with inhibitor A
=
KM; with inhibitor B =
Select the type of inhibition displayed by inhibitor B.
O uncompetitive
O competitive
Ononcompetitive
μΜ
μΜ
μM
![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.
[S] (µm)
3
5
10
30
90
1/V Slope = KM/Vmax
Intercept = -1/KM
Vo (μmol/min); with no
inhibitor
10.4
14.5
22.5
33.8
0
40.5
Intercept = 1/Vmax
1/[S]
Vo (μmol/min); with
inhibitor A
4.1
6.4
11.3
22.6
33.8
V (μmol/min); with
inhibitor B
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.
2.1
2.9
4.5
6.8
8.1](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fc94cb5d1-997a-49d0-b0ef-9ec02bf0a187%2F13f9d616-b75d-4902-98a8-0f4cddbae0f1%2Fypx398_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.
[S] (µm)
3
5
10
30
90
1/V Slope = KM/Vmax
Intercept = -1/KM
Vo (μmol/min); with no
inhibitor
10.4
14.5
22.5
33.8
0
40.5
Intercept = 1/Vmax
1/[S]
Vo (μmol/min); with
inhibitor A
4.1
6.4
11.3
22.6
33.8
V (μmol/min); with
inhibitor B
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.
2.1
2.9
4.5
6.8
8.1
Expert Solution
This question has been solved!
Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.
This is a popular solution!
Trending now
This is a popular solution!
Step by step
Solved in 5 steps with 5 images
Recommended textbooks for you
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
ISBN:
9781319114671
Author:
Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:
W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:
9781464126116
Author:
David L. Nelson, Michael M. Cox
Publisher:
W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul…
Biochemistry
ISBN:
9781118918401
Author:
Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:
WILEY
Biochemistry
Biochemistry
ISBN:
9781305961135
Author:
Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:
Cengage Learning
Biochemistry
Biochemistry
ISBN:
9781305577206
Author:
Reginald H. Garrett, Charles M. Grisham
Publisher:
Cengage Learning
Fundamentals of General, Organic, and Biological …
Biochemistry
ISBN:
9780134015187
Author:
John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:
PEARSON