Passage 1 (Questions 1-4) Human immunodeficiency virus 1 (HIV-1) protease inhibitors have been successful at lowering HIV-1 levels and blocking the onset of acquired immune deficiency syndrome (AIDS). However, because HIV-1 mutants are developing resistance to current protease inhibitors, new inhibitors such as Compound 1 (molar mass: 483.5 g-mol-¹) are being tested. N Compound 1 Compound 1 has been shown to inhibit HIV-1 protease with K₁ = 60.3 μM (Table 1). K; is the dissociation constant for the enzyme-bound inhibitor, which is either El or ESI, depending on the type of inhibitor. The peptide substrate for HIV-1 protease is IRKILFLDG. HIV-1 protease hydrolyzes only the peptide bond after leucine and before phenylalanine. Compound 1 (μm) 0 60.0 120 Table 1 Kinetic Parameters of HIV-1 Protease with and without Compound 1 N H Км Ксач Км K₁ (mM) (S¹) (mM-¹ s¹) (HM) 1.678 0.250 00.149 0.832 0.126 0.151 60.3 0.430 0.064 0.149 60.3 Note: HIV-1 protease follows Michaelis-Menten kinetics. N N= N A Lineweaver-Burk plot of V.¹ versus [S]-1, both without Compound 1 and with different concentrations of Compound 1, generates a set of parallel straight lines with positive slopes. Adapted from T. Sperka, J. Pitlik, P. Bagossi, and J. Tösner, Bioorganic & Medicinal Chemistry Letters. ©2005 Elsevier Inc. Question 2 If only [1] is increased, then [ESI] or [E] increases. This is an example of: O A. the Bose-Einstein Principle. OB. the Heisenberg Uncertainty Principle. O c. the Le Châtelier's Principle. OD. the Pauli Exclusion Principle. OA. 33.5 and 15.7 Question 3 Which structural change to Compound 1 would make it more water soluble? OB. 75 and 30.1 O C. 150 and 60.3 O A. Replacing benzene CH with N in the ring OB. Replacing C=0 with C=CH₂ OC. Replacing N-N-N with CH-CH=CH OD. Replacing NH with NCH3 O D. 300 and 120.6 Question 4 In μM-s¹ and μM, what should the approximate values of kcat/KM and K, be, respectively, when [1] = 180 μM?
Passage 1 (Questions 1-4) Human immunodeficiency virus 1 (HIV-1) protease inhibitors have been successful at lowering HIV-1 levels and blocking the onset of acquired immune deficiency syndrome (AIDS). However, because HIV-1 mutants are developing resistance to current protease inhibitors, new inhibitors such as Compound 1 (molar mass: 483.5 g-mol-¹) are being tested. N Compound 1 Compound 1 has been shown to inhibit HIV-1 protease with K₁ = 60.3 μM (Table 1). K; is the dissociation constant for the enzyme-bound inhibitor, which is either El or ESI, depending on the type of inhibitor. The peptide substrate for HIV-1 protease is IRKILFLDG. HIV-1 protease hydrolyzes only the peptide bond after leucine and before phenylalanine. Compound 1 (μm) 0 60.0 120 Table 1 Kinetic Parameters of HIV-1 Protease with and without Compound 1 N H Км Ксач Км K₁ (mM) (S¹) (mM-¹ s¹) (HM) 1.678 0.250 00.149 0.832 0.126 0.151 60.3 0.430 0.064 0.149 60.3 Note: HIV-1 protease follows Michaelis-Menten kinetics. N N= N A Lineweaver-Burk plot of V.¹ versus [S]-1, both without Compound 1 and with different concentrations of Compound 1, generates a set of parallel straight lines with positive slopes. Adapted from T. Sperka, J. Pitlik, P. Bagossi, and J. Tösner, Bioorganic & Medicinal Chemistry Letters. ©2005 Elsevier Inc. Question 2 If only [1] is increased, then [ESI] or [E] increases. This is an example of: O A. the Bose-Einstein Principle. OB. the Heisenberg Uncertainty Principle. O c. the Le Châtelier's Principle. OD. the Pauli Exclusion Principle. OA. 33.5 and 15.7 Question 3 Which structural change to Compound 1 would make it more water soluble? OB. 75 and 30.1 O C. 150 and 60.3 O A. Replacing benzene CH with N in the ring OB. Replacing C=0 with C=CH₂ OC. Replacing N-N-N with CH-CH=CH OD. Replacing NH with NCH3 O D. 300 and 120.6 Question 4 In μM-s¹ and μM, what should the approximate values of kcat/KM and K, be, respectively, when [1] = 180 μM?
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
![Passage 1 (Questions 1-4)
Human immunodeficiency virus 1 (HIV-1) protease inhibitors have been
successful at lowering HIV-1 levels and blocking the onset of acquired
immune deficiency syndrome (AIDS). However, because HIV-1 mutants
are developing resistance to current protease inhibitors, new inhibitors
such as Compound 1 (molar mass: 483.5 g-mol-¹) are being tested.
N
Compound 1
Compound 1 has been shown to inhibit HIV-1 protease with K₁ = 60.3
μM (Table 1). K; is the dissociation constant for the enzyme-bound
inhibitor, which is either El or ESI, depending on the type of inhibitor. The
peptide substrate for HIV-1 protease is IRKILFLDG. HIV-1 protease
hydrolyzes only the peptide bond after leucine and before
phenylalanine.
Compound 1
(μm)
0
60.0
120
Table 1 Kinetic Parameters of HIV-1 Protease with and without
Compound 1
N
H
Км
Ксач
Км
K₁
(mM) (S¹) (mM-¹ s¹) (HM)
1.678 0.250
00.149
0.832 0.126 0.151 60.3
0.430 0.064 0.149 60.3
Note: HIV-1 protease follows Michaelis-Menten kinetics.
N
N=
N
A Lineweaver-Burk plot of V.¹ versus [S]-1, both without Compound 1
and with different concentrations of Compound 1, generates a set of
parallel straight lines with positive slopes.
Adapted from T. Sperka, J. Pitlik, P. Bagossi, and J. Tösner, Bioorganic & Medicinal Chemistry Letters. ©2005
Elsevier Inc.
Question 2
If only [1] is increased, then [ESI] or [E] increases. This is an example of:
O A. the Bose-Einstein Principle.
OB. the Heisenberg Uncertainty Principle.
O c. the Le Châtelier's Principle.
OD. the Pauli Exclusion Principle.
OA. 33.5 and 15.7
Question 3
Which structural change to Compound 1 would make it more water
soluble?
OB. 75 and 30.1
O C. 150 and 60.3
O A. Replacing benzene CH with N in the ring
OB. Replacing C=0 with C=CH₂
OC. Replacing N-N-N with CH-CH=CH
OD. Replacing NH with NCH3
O D. 300 and 120.6
Question 4
In μM-s¹ and μM, what should the approximate values of kcat/KM and
K, be, respectively, when [1] = 180 μM?](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F8632ab95-12c0-43a1-a9c9-ae2ef8531ad4%2F3460dec4-e32c-41f9-8d51-9ed177db3f26%2Fd8i7mb_processed.jpeg&w=3840&q=75)
Transcribed Image Text:Passage 1 (Questions 1-4)
Human immunodeficiency virus 1 (HIV-1) protease inhibitors have been
successful at lowering HIV-1 levels and blocking the onset of acquired
immune deficiency syndrome (AIDS). However, because HIV-1 mutants
are developing resistance to current protease inhibitors, new inhibitors
such as Compound 1 (molar mass: 483.5 g-mol-¹) are being tested.
N
Compound 1
Compound 1 has been shown to inhibit HIV-1 protease with K₁ = 60.3
μM (Table 1). K; is the dissociation constant for the enzyme-bound
inhibitor, which is either El or ESI, depending on the type of inhibitor. The
peptide substrate for HIV-1 protease is IRKILFLDG. HIV-1 protease
hydrolyzes only the peptide bond after leucine and before
phenylalanine.
Compound 1
(μm)
0
60.0
120
Table 1 Kinetic Parameters of HIV-1 Protease with and without
Compound 1
N
H
Км
Ксач
Км
K₁
(mM) (S¹) (mM-¹ s¹) (HM)
1.678 0.250
00.149
0.832 0.126 0.151 60.3
0.430 0.064 0.149 60.3
Note: HIV-1 protease follows Michaelis-Menten kinetics.
N
N=
N
A Lineweaver-Burk plot of V.¹ versus [S]-1, both without Compound 1
and with different concentrations of Compound 1, generates a set of
parallel straight lines with positive slopes.
Adapted from T. Sperka, J. Pitlik, P. Bagossi, and J. Tösner, Bioorganic & Medicinal Chemistry Letters. ©2005
Elsevier Inc.
Question 2
If only [1] is increased, then [ESI] or [E] increases. This is an example of:
O A. the Bose-Einstein Principle.
OB. the Heisenberg Uncertainty Principle.
O c. the Le Châtelier's Principle.
OD. the Pauli Exclusion Principle.
OA. 33.5 and 15.7
Question 3
Which structural change to Compound 1 would make it more water
soluble?
OB. 75 and 30.1
O C. 150 and 60.3
O A. Replacing benzene CH with N in the ring
OB. Replacing C=0 with C=CH₂
OC. Replacing N-N-N with CH-CH=CH
OD. Replacing NH with NCH3
O D. 300 and 120.6
Question 4
In μM-s¹ and μM, what should the approximate values of kcat/KM and
K, be, respectively, when [1] = 180 μM?
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