3. (а) 0.0050 M operate at one-quarter of its maximum rate? At what substrate concentration would an enzyme with a kcat of 30.0 s1 and a KM of (b) trations [So]: ½ Km, 2 Km, and 10 KM. Determine the fraction of Vmax that would be obtained at the following substrate concen- (c) ( 1 (HIV-1) has been the object of innumerable studies to develop effective chemotherapeutic agents. It has been shown that p6* known as the late assembly protein is an inhibitor of HIV protease. An assay was developed using an artificial polypeptide substrate containing a p-nitrophenylalanine residue at the cleavage point that undergoes a small change in absorption at 295 nm upon bond hydrolysis that could be followed spectrophotometrically. The cleavage of the peptide bond is shown schematically on the right. Results of the assay are given in the table below. The protease of the human immunodeficiency virus- Lys NH2 Ala Nle Arg Ala Val-Nle-NH-CH-C–NH-Glu CH2 Lys NH2 Ala NO2 Nle H2O - HIV-1 protease Ala Vo (nmole/min) in presence of 10рМ рб* pro- tein Arg Vo Val-Nle-NH-CH-COC- + NH-Glu [S] (µM) (nmole/min) CH2 10 4.63 2.70 15 5.88 3.46 20 6.94 4.74 NO2 25 9.26 6.06 30 10.78 6.49 40 12.14 8.06 50 14.93 9.71 Construct a Lineweaver-Burk plot to determine what type of an inhibitor the p6* protein is. Extract from the plot Vmax, KM, and the Ki of the protein.
3. (а) 0.0050 M operate at one-quarter of its maximum rate? At what substrate concentration would an enzyme with a kcat of 30.0 s1 and a KM of (b) trations [So]: ½ Km, 2 Km, and 10 KM. Determine the fraction of Vmax that would be obtained at the following substrate concen- (c) ( 1 (HIV-1) has been the object of innumerable studies to develop effective chemotherapeutic agents. It has been shown that p6* known as the late assembly protein is an inhibitor of HIV protease. An assay was developed using an artificial polypeptide substrate containing a p-nitrophenylalanine residue at the cleavage point that undergoes a small change in absorption at 295 nm upon bond hydrolysis that could be followed spectrophotometrically. The cleavage of the peptide bond is shown schematically on the right. Results of the assay are given in the table below. The protease of the human immunodeficiency virus- Lys NH2 Ala Nle Arg Ala Val-Nle-NH-CH-C–NH-Glu CH2 Lys NH2 Ala NO2 Nle H2O - HIV-1 protease Ala Vo (nmole/min) in presence of 10рМ рб* pro- tein Arg Vo Val-Nle-NH-CH-COC- + NH-Glu [S] (µM) (nmole/min) CH2 10 4.63 2.70 15 5.88 3.46 20 6.94 4.74 NO2 25 9.26 6.06 30 10.78 6.49 40 12.14 8.06 50 14.93 9.71 Construct a Lineweaver-Burk plot to determine what type of an inhibitor the p6* protein is. Extract from the plot Vmax, KM, and the Ki of the protein.
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
![3. (а)
0.0050 M operate at one-quarter of its maximum rate?
At what substrate concentration would an enzyme with a kcat of 30.0 s-1 and a Km of
(b)
trations [So]: ½ Km, 2 KM, and 10 KM.
Determine the fraction of Vmax that would be obtained at the following substrate concen-
(c) (
1 (HIV-1) has been the object of innumerable studies to develop
effective chemotherapeutic agents. It has been shown that p6*
known as the late assembly protein is an inhibitor of HIV protease.
An assay was developed using an artificial polypeptide substrate
containing a p-nitrophenylalanine residue at the cleavage point
that undergoes a small change in absorption at 295 nm upon bond
hydrolysis that could be followed spectrophotometrically. The
cleavage of the peptide bond is shown schematically on the right.
Results of the assay are given in the table below.
The protease of the human immunodeficiency virus-
Lys
NH2
Ala
Nle
Arg
Ala
Val-Nle-NH-CH-
C-NH-Glu
CH2
Lys
NH2
Ala
NO2
Nle
H2OH
NHIV-1 protease
Ala
Vo (nmole/min)
in presence of
10рМ рб* pro-
Arg
Vo
Val-Nle-NH-CH-CO0-
+ NH-Glu
[S]
(nmole/min)
(иM)
CH2
tein
10
4.63
2.70
15
5.88
3.46
20
6.94
4.74
NO2
25
9.26
6.06
30
10.78
6.49
40
12.14
8.06
50
14.93
9.71
Construct a Lineweaver-Burk plot to determine what type of an inhibitor the p6* protein is. Extract from
the plot Vmax, Km, and the Ki of the protein.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F7e3218aa-1b65-42a2-9071-7edb43c3a555%2Fc5330f81-50e9-45b7-8d8e-512617ffcdf0%2Fy06fbw7_processed.png&w=3840&q=75)
Transcribed Image Text:3. (а)
0.0050 M operate at one-quarter of its maximum rate?
At what substrate concentration would an enzyme with a kcat of 30.0 s-1 and a Km of
(b)
trations [So]: ½ Km, 2 KM, and 10 KM.
Determine the fraction of Vmax that would be obtained at the following substrate concen-
(c) (
1 (HIV-1) has been the object of innumerable studies to develop
effective chemotherapeutic agents. It has been shown that p6*
known as the late assembly protein is an inhibitor of HIV protease.
An assay was developed using an artificial polypeptide substrate
containing a p-nitrophenylalanine residue at the cleavage point
that undergoes a small change in absorption at 295 nm upon bond
hydrolysis that could be followed spectrophotometrically. The
cleavage of the peptide bond is shown schematically on the right.
Results of the assay are given in the table below.
The protease of the human immunodeficiency virus-
Lys
NH2
Ala
Nle
Arg
Ala
Val-Nle-NH-CH-
C-NH-Glu
CH2
Lys
NH2
Ala
NO2
Nle
H2OH
NHIV-1 protease
Ala
Vo (nmole/min)
in presence of
10рМ рб* pro-
Arg
Vo
Val-Nle-NH-CH-CO0-
+ NH-Glu
[S]
(nmole/min)
(иM)
CH2
tein
10
4.63
2.70
15
5.88
3.46
20
6.94
4.74
NO2
25
9.26
6.06
30
10.78
6.49
40
12.14
8.06
50
14.93
9.71
Construct a Lineweaver-Burk plot to determine what type of an inhibitor the p6* protein is. Extract from
the plot Vmax, Km, and the Ki of the protein.
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 2 steps with 3 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