1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 им. a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? c. Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and KM for the enzyme. [S] (mM) (1) V. (2) V. (3) V. [(umol/(ml.s)] [(umol/(ml.s)] [(umol/(ml.s)] 7.6 4.4 6.6 14.6 8.6 11.4 8. 26.6 16.4 17.8 16 45.8 29.8 24.6 24 60 40.8 28.2
1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 им. a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? c. Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and KM for the enzyme. [S] (mM) (1) V. (2) V. (3) V. [(umol/(ml.s)] [(umol/(ml.s)] [(umol/(ml.s)] 7.6 4.4 6.6 14.6 8.6 11.4 8. 26.6 16.4 17.8 16 45.8 29.8 24.6 24 60 40.8 28.2
Introduction to Chemical Engineering Thermodynamics
8th Edition
ISBN:9781259696527
Author:J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Publisher:J.M. Smith Termodinamica en ingenieria quimica, Hendrick C Van Ness, Michael Abbott, Mark Swihart
Chapter1: Introduction
Section: Chapter Questions
Problem 1.1P
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![1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two
columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each
reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001
им.
a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve.
b. Provide the type of inhibition for both?
c. Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3).
d. Calculate the reaction Kcat for the Control in experiment (1).
e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax
and KM for the enzyme.
[S] (mM)
(1) V.
(2) V.
(3) V.
[(umol/(ml.s)]
[(umol/(ml.s)]
[(umol/(ml.s)]
7.6
4.4
6.6
14.6
8.6
11.4
8.
26.6
16.4
17.8
16
45.8
29.8
24.6
24
60
40.8
28.2](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F456ceb0e-8de7-4334-80ce-c73ec45a3918%2F16b93004-1cac-414d-a729-73b4b70b6c94%2Fv14mum6.jpeg&w=3840&q=75)
Transcribed Image Text:1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two
columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each
reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001
им.
a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve.
b. Provide the type of inhibition for both?
c. Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3).
d. Calculate the reaction Kcat for the Control in experiment (1).
e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax
and KM for the enzyme.
[S] (mM)
(1) V.
(2) V.
(3) V.
[(umol/(ml.s)]
[(umol/(ml.s)]
[(umol/(ml.s)]
7.6
4.4
6.6
14.6
8.6
11.4
8.
26.6
16.4
17.8
16
45.8
29.8
24.6
24
60
40.8
28.2
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