a) ; Construct a Lineweaver -Burk plot using the kinetic data shown in Table 1.. Determine Vmax and Km for the uninhibited enzyme and inhibited enzyme. .

Biochemistry
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Chapter1: Biochemistry: An Evolving Science
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Table below shows the kinetic data obtained for an enzyme in the absence of any inhibitor (1), and
in the presence of an inhibitor (2), at a concentration of 7.0 mM. Assume the total enzyme
concentration, [E]T, is the same for each experiment.
Table 1
[S]
(mM)
Vo
Vo
{umol/(mL•s)}
{umol/(mL•s)}
Without Inhibitor
With Inhibitor
(1)
3.8
(2)
2.2
1
2
7.3
4.3
4
13.3
8.2
8
22.9
14.9
12
30.0
20.4
a); Construct a Lineweaver -Burk plot using the kinetic data shown in Table 1.
Determine Vmax and Km for the uninhibited enzyme and inhibited enzyme.
Transcribed Image Text:Table below shows the kinetic data obtained for an enzyme in the absence of any inhibitor (1), and in the presence of an inhibitor (2), at a concentration of 7.0 mM. Assume the total enzyme concentration, [E]T, is the same for each experiment. Table 1 [S] (mM) Vo Vo {umol/(mL•s)} {umol/(mL•s)} Without Inhibitor With Inhibitor (1) 3.8 (2) 2.2 1 2 7.3 4.3 4 13.3 8.2 8 22.9 14.9 12 30.0 20.4 a); Construct a Lineweaver -Burk plot using the kinetic data shown in Table 1. Determine Vmax and Km for the uninhibited enzyme and inhibited enzyme.
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