Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to the enzyme’s function.  Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.

Biomedical Instrumentation Systems
1st Edition
ISBN:9781133478294
Author:Chatterjee
Publisher:Chatterjee
Chapter9: Instrumentation In Blood Circulation
Section: Chapter Questions
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Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to the enzyme’s function.  Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.  

0.5
0.0
1.0
0.5
1.0
0.5
0.0
1
[F6P] (mM)
Relative velocity, v/V
Relative velocity, v/V
Relative velocity, v/V
Transcribed Image Text:0.5 0.0 1.0 0.5 1.0 0.5 0.0 1 [F6P] (mM) Relative velocity, v/V Relative velocity, v/V Relative velocity, v/V
PFK-1 protein
Wild type
Vmax
Km fructose 6-phosphate
KI ATP
Ki citrate
59.27
0.83mM
0.96
0.4
R48C
58.19
0.84mM
1.19
>4
N426S
67.41
0.82mM
>3
0.31
D546N
30.6
2.04mM
0.68
1.4
The data in the table are derived from the enzyme assays in the graphs below. The red squares
represent the R48C variant, the blue rightside up triangles represent N426S, the green upside
down triangles represent D546N, and the black circles represent wild type PFK-1. Fructose 6-
phosphate and ATP, the substrates, are present in all assays. In graph d, the velocity of PFK-1 is
being measured with respect to varying citrate concentration. In graph e, the velocity of PFK-1
is being measured with respect to varying ATP concentration. In graph f, the velocity of PFK-1 is
being measured with respect to varying F6P concentration.
Transcribed Image Text:PFK-1 protein Wild type Vmax Km fructose 6-phosphate KI ATP Ki citrate 59.27 0.83mM 0.96 0.4 R48C 58.19 0.84mM 1.19 >4 N426S 67.41 0.82mM >3 0.31 D546N 30.6 2.04mM 0.68 1.4 The data in the table are derived from the enzyme assays in the graphs below. The red squares represent the R48C variant, the blue rightside up triangles represent N426S, the green upside down triangles represent D546N, and the black circles represent wild type PFK-1. Fructose 6- phosphate and ATP, the substrates, are present in all assays. In graph d, the velocity of PFK-1 is being measured with respect to varying citrate concentration. In graph e, the velocity of PFK-1 is being measured with respect to varying ATP concentration. In graph f, the velocity of PFK-1 is being measured with respect to varying F6P concentration.
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