Problem 2. Competitive inhibitors are commonly used to make pharmaceuticals. Some cancer drugs act as competitive inhibitors to reduce the undesired effects of oncogenic kinases. The figure below shows V-S profiles of a kinase enzyme in the presence of two different inhibitors (Ij and I½) competing with the substrate. The enzyme parameters, Km and Vmax, are known to be 0.8 and 1.2 nM/s, respectively. Determine Equilibrium constants, K1 and K2, associated with the first and second inhibitors. 0.7 0.6 0.5 0.4 0.3 0.1nM 11+ 0.1nM 12 0.15nM 11 + 0.05nM 2 0.2 0.1 0.5 15 2.5 3.5 [S] (nM) (s/Wu) °A

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Chapter1: Biochemistry: An Evolving Science
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Problem 2. Competitive inhibitors are commonly used to make pharmaceuticals. Some cancer drugs act as
competitive inhibitors to reduce the undesired effects of oncogenic kinases. The figure below shows V-S
profiles of a kinase enzyme in the presence of two different inhibitors (Ij and I) competing with the substrate.
The enzyme parameters, Km and Vmax, are known to be 0.8 and 1.2 nM/s, respectively. Determine Equilibrium
constants, K1 and K2, associated with the first and second inhibitors.
0.7
0.6
0.5
0.4
0.3
--0.1nM 11+0.1nM 12
..... 0.15nM 11 +0.05nM 12
0.2
0.1
0.5
1.5
2
2.5
3.5
[S] (nM)
(s/wu) °A
Transcribed Image Text:Problem 2. Competitive inhibitors are commonly used to make pharmaceuticals. Some cancer drugs act as competitive inhibitors to reduce the undesired effects of oncogenic kinases. The figure below shows V-S profiles of a kinase enzyme in the presence of two different inhibitors (Ij and I) competing with the substrate. The enzyme parameters, Km and Vmax, are known to be 0.8 and 1.2 nM/s, respectively. Determine Equilibrium constants, K1 and K2, associated with the first and second inhibitors. 0.7 0.6 0.5 0.4 0.3 --0.1nM 11+0.1nM 12 ..... 0.15nM 11 +0.05nM 12 0.2 0.1 0.5 1.5 2 2.5 3.5 [S] (nM) (s/wu) °A
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