At what substrate concentration would an enzyme with a kcat of 30.0 s-1 and a Km of 3. (а) 0.0050 M operate at one-quarter of its maximum rate? (b) trations [So]: ½ Km, 2 Km, and 10 Km. Determine the fraction of Vmax that would be obtained at the following substrate concen-

Chemistry & Chemical Reactivity
10th Edition
ISBN:9781337399074
Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Chapter14: Chemical Kinetics: The Rates Of Chemical Reactions
Section14.7: Reaction Mechanisms
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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-Ċ–NH-Glu
CH2
Lys
NH2
Ala
NO2
Nle
H2ON HIV-1 protease
Ala
Vo (nmole/min)
Arg
Vo
presence of
Val-Nle-NH-CH-COO-
+ NH-Glu
[S]
(nmole/min)
(µM)
10µM p6* pro-
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
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-Ċ–NH-Glu CH2 Lys NH2 Ala NO2 Nle H2ON HIV-1 protease Ala Vo (nmole/min) Arg Vo presence of Val-Nle-NH-CH-COO- + NH-Glu [S] (nmole/min) (µM) 10µM p6* pro- 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
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