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Enzyme Kinetics and Inhibition, Part 1 (worksheet for laboratory exercise 5) Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.) for all six of these experiments: 1/ V. (1) 0 mM O mM 0 mM 0 mM 0 mM [S] 0.1 mM 0.2 mM Vo 0.3333 0.50 1/[S] 33333 mM per minute 0.3 mM 0.4 mM 0.5 mM 0.60 0.666666666667 0.714285714286 0.1 mM 0.1 mM 0.20 0.2 mM 0.3 mM 0.1 mM 0.333333333333 0.428571428571 0.50 0.1 mM 0.1 mM 0.4 mM 0.5 mM 0.1 mM 0.1 mM 0.555555555556 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.3 mM 0.142857142857 0.25 0.2 mM 0.3 mM 0.333333333333 0.40 0.454545454545 0.111111111111 0.20 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.3 mM 0.272727272727 0.333333333333 0.384615384615 0.3 mM 0.3 mM 0.3 mM 0.40 mM 0.090909090909 0.40 mM 0.40 mM 0.40 mM 0.40 mM 0.5 mM 0.5 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.166666666667 0.230769230769 0.285714285714 0.333333333333 0.076923076923 0.142857142857. 0.20 0.25 0.5 mM 0.5 mM 0.5 mM Construct a Michaelis-Menten plot, and a Lineweaver-Burk plot, for all six of these experiments on the same graph (for each plot). Calculate the Vmax, the Km, and the slope (Km/Vmax) for the control (with [I] = 0 mM) and for each non-zero concentration of inhibitor A ([I] = 0.1, 0.2, 0.3, 0.4, and 0.5 mM). Which type of reversible enzyme inhibition is illustrated by inhibitor A? 0.5 mM 0.294117647059

Enzyme Kinetics and Inhibition, Part 1 (worksheet for laboratory exercise 5) Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.) for all six of these experiments: 1/ V. (1) 0 mM O mM 0 mM 0 mM 0 mM [S] 0.1 mM 0.2 mM Vo 0.3333 0.50 1/[S] 33333 mM per minute 0.3 mM 0.4 mM 0.5 mM 0.60 0.666666666667 0.714285714286 0.1 mM 0.1 mM 0.20 0.2 mM 0.3 mM 0.1 mM 0.333333333333 0.428571428571 0.50 0.1 mM 0.1 mM 0.4 mM 0.5 mM 0.1 mM 0.1 mM 0.555555555556 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.3 mM 0.142857142857 0.25 0.2 mM 0.3 mM 0.333333333333 0.40 0.454545454545 0.111111111111 0.20 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.3 mM 0.272727272727 0.333333333333 0.384615384615 0.3 mM 0.3 mM 0.3 mM 0.40 mM 0.090909090909 0.40 mM 0.40 mM 0.40 mM 0.40 mM 0.5 mM 0.5 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.166666666667 0.230769230769 0.285714285714 0.333333333333 0.076923076923 0.142857142857. 0.20 0.25 0.5 mM 0.5 mM 0.5 mM Construct a Michaelis-Menten plot, and a Lineweaver-Burk plot, for all six of these experiments on the same graph (for each plot). Calculate the Vmax, the Km, and the slope (Km/Vmax) for the control (with [I] = 0 mM) and for each non-zero concentration of inhibitor A ([I] = 0.1, 0.2, 0.3, 0.4, and 0.5 mM). Which type of reversible enzyme inhibition is illustrated by inhibitor A? 0.5 mM 0.294117647059

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
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Enzyme Kinetics and Inhibition, Part 1 (worksheet for laboratory exercise 5) Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.) for all six of these experiments: 1/ V. (1) 0 mM O mM 0 mM 0 mM 0 mM [S] 0.1 mM 0.2 mM Vo 0.3333 0.50 1/[S] 33333 mM per minute 0.3 mM 0.4 mM 0.5 mM 0.60 0.666666666667 0.714285714286 0.1 mM 0.1 mM 0.20 0.2 mM 0.3 mM 0.1 mM 0.333333333333 0.428571428571 0.50 0.1 mM 0.1 mM 0.4 mM 0.5 mM 0.1 mM 0.1 mM 0.555555555556 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.3 mM 0.142857142857 0.25 0.2 mM 0.3 mM 0.333333333333 0.40 0.454545454545 0.111111111111 0.20 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.3 mM 0.272727272727 0.333333333333 0.384615384615 0.3 mM 0.3 mM 0.3 mM 0.40 mM 0.090909090909 0.40 mM 0.40 mM 0.40 mM 0.40 mM 0.5 mM 0.5 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.166666666667 0.230769230769 0.285714285714 0.333333333333 0.076923076923 0.142857142857. 0.20 0.25 0.5 mM 0.5 mM 0.5 mM Construct a Michaelis-Menten plot, and a Lineweaver-Burk plot, for all six of these experiments on the same graph (for each plot). Calculate the Vmax, the Km, and the slope (Km/Vmax) for the control (with [I] = 0 mM) and for each non-zero concentration of inhibitor A ([I] = 0.1, 0.2, 0.3, 0.4, and 0.5 mM). Which type of reversible enzyme inhibition is illustrated by inhibitor A? 0.5 mM 0.294117647059
Transcribed Image Text:Enzyme Kinetics and Inhibition, Part 1 (worksheet for laboratory exercise 5) Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.) for all six of these experiments: 1/ V. (1) 0 mM O mM 0 mM 0 mM 0 mM [S] 0.1 mM 0.2 mM Vo 0.3333 0.50 1/[S] 33333 mM per minute 0.3 mM 0.4 mM 0.5 mM 0.60 0.666666666667 0.714285714286 0.1 mM 0.1 mM 0.20 0.2 mM 0.3 mM 0.1 mM 0.333333333333 0.428571428571 0.50 0.1 mM 0.1 mM 0.4 mM 0.5 mM 0.1 mM 0.1 mM 0.555555555556 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.3 mM 0.142857142857 0.25 0.2 mM 0.3 mM 0.333333333333 0.40 0.454545454545 0.111111111111 0.20 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.3 mM 0.272727272727 0.333333333333 0.384615384615 0.3 mM 0.3 mM 0.3 mM 0.40 mM 0.090909090909 0.40 mM 0.40 mM 0.40 mM 0.40 mM 0.5 mM 0.5 mM 0.2 mM 0.3 mM 0.4 mM 0.5 mM 0.1 mM 0.2 mM 0.3 mM 0.4 mM 0.166666666667 0.230769230769 0.285714285714 0.333333333333 0.076923076923 0.142857142857. 0.20 0.25 0.5 mM 0.5 mM 0.5 mM Construct a Michaelis-Menten plot, and a Lineweaver-Burk plot, for all six of these experiments on the same graph (for each plot). Calculate the Vmax, the Km, and the slope (Km/Vmax) for the control (with [I] = 0 mM) and for each non-zero concentration of inhibitor A ([I] = 0.1, 0.2, 0.3, 0.4, and 0.5 mM). Which type of reversible enzyme inhibition is illustrated by inhibitor A? 0.5 mM 0.294117647059
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