Compute using the Ki formula An attempt was made to inhibit Enzyme X by adding compounds M and L. The resultsare summarized in the table below:Which of the 2 compounds is the best inhibitor of Enzyme X? Show your computation.Assume equal concentrations of compound M and compound L.Km apparent,VmaxType of Inhibitionapparent,umol/LmM/minCompound M5.0 x 10-40.30Non-competitiveCompound L2.5 x 10-20.40CompetitiveKmVmaxWithout inhibitor 5.0 x 10-40.40

Inhibitors are substances that inhibit the enzyme and decrease enzyme activity. Inhibitors are…

Answered: An attempt was made to inhibit Enzyme X…

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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Similar questions

If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?
In an enzyme experiment, when the enzyme is added only to the substrate, the Vmax value is 0.828 and the Km value is 17.76. When the substrate and activator are added to this enzyme, the Vmax is 0.964 and the Km value is 10.6066. When substrate and inhibitor are added to the enzyme, the Vmax value is 0.550 and the Km value is 11.34. Estimate the effect of the substance added. Are these substances suitable activators/inhibitors for the laccase enzyme?
The following data was obtained during kinetic analysis of an enzyme with and without an inhibitor. Substrate concentration (mM) Reaction rate without inhibitor (µM/s) Reaction rate with inhibitor (µM/s) 10 28 12 20 50 23 40 83 42 60 107 58 100 139 83 200 179 125 300 197 150 400 209 167 560 227 197 How do you calculate the KM for the enzyme in the absence of an inhibitor. And how do you calculate kcat with the given enzymatic concentration of 5 µM.
Q is an analog of substrate A that binds to enzyme X and produces the following kinetics:[A] V0 (µmole/ml/min) [Q] = 0 [Q] = 0.5 µM [Q] = 2 µM1 µM 10 7 43 µM 20 16 1010 µM 35 31 2330 µM 43 41 3680 µM 47 46 43a) Plot the data in Lineweaver Burk plot form (Hint: there should be three plots of dataon your graph) and determine the following: the KM and Vmax of the enzyme X in theabsence of Q, and the KMapp the Vmaxapp at each concentration of Q. b) What type of inhibition is this?c) Calculate the inhibition constant (Ki) for Compound Q
What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is impact of the lower V max on the amount of product formed ? If the lower value of black resulting in the new plot (red curve) is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible ? And why?
Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Line (B) represents ____________. A. an enzyme-catalyzed reaction in the absence of any inhibitor. B. an enzyme-catalyzed reaction in the presence of a competitive inhibitor. C. an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor. D. an enzyme-catalyzed reaction in the presence of a noncompetitive, or mixed, inhibitor.
Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the Km of the reaction represented by Line (B).
Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Which of the following statements is true? Select any/all answers that apply. A. Both types of inhibitor mediate a slope effect on the Lineweaver-Burke plot. B. Both types of inhibitor decrease the apparent Vmax for this enzyme-catalyzed reaction. C. Both types of inhibitor alter the apparent Km of this enzyme-catalyzed reaction. D. Lines (A) and (C) share the same X-intercept, indicating that the noncompetitive inhibitor decreases the apparent Km of this enzyme-catalyzed reaction. E. Lines (A) and (C)…
Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the catalytic efficiency of the reaction represented by Line (A).
Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. QUESTION: Line (A) represents ____________. A. an enzyme-catalyzed reaction in the absence of any inhibitor. B. an enzyme-catalyzed reaction in the presence of a competitive inhibitor. C. an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor. D. an enzyme-catalyzed reaction in the presence of a noncompetitive, or mixed, inhibitor.
Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the Vmax of the reaction represented by Line (C). Show all mathematical work, please.
a. What is the Vmax of this enzyme WITHOUT inhibitor? Please show your work. b. What is the Km of this enzyme WITHOUT inhibitor? Please show your work. c. The specificity constant of enzyme X is 8 x 10^7 /(M * seconds) What is the kcat of enzyme X WITHOUT inhibitor? Please show your work d. What was the concentration of enzyme used for measuring the kinetics of enzyme X WITHOUT inhibitor? Please show your work

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