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Table 1 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]r, 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 7.3 13.3 22.9 4.3 4 8.2 8 14.9 12 30.0 20.4

Table 1 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]r, 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 7.3 13.3 22.9 4.3 4 8.2 8 14.9 12 30.0 20.4

Biochemistry
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
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Table 1 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 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. a) Determine Vmax and Km for the uninhibited enzyme and inhibited enzyme. b) i Determine the type of inhibition. Determine the dissociation constant, K;, for the inhibitor binding to the enzyme. Show your working.
Transcribed Image Text:Table 1 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 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. a) Determine Vmax and Km for the uninhibited enzyme and inhibited enzyme. b) i Determine the type of inhibition. Determine the dissociation constant, K;, for the inhibitor binding to the enzyme. Show your working.
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