33.. Using linear regression analysis, determine the values of Vmax and KM of the enzyme in the PRESENCE ofinhibitor: (Express your answer in 3 decimal places, do NOT include the units)V max%3DKM =What is the MODE of inhibition exerted by DEDS? You were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newly discovered enzymeknown as BILISTASE. The kinetics data are shown below:[Substrate, uM]Vo with DEDS (µM/min)Vo without DEDS (uM/min)3.3330.7741.1964.0000.8771.3165.0001.0121.46210.0001.4621.88020.0001.8802.193

The enzyme binds to the substrate form an enzyme-substrate complex in an enzyme-catalyzed reaction.…

Answered: Using linear regression analysis,…

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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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?
Given the following data in enzyme-catalyzed reaction, what is the Vm, Km and type of inhibition of Experiment A?
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.
You are attempting to determine KM by measuring the reaction velocity at different substrate concentrations, but you do not realize that the substrate tends to precipitate under the experimental conditions you have chosen. How would this affect your measurement of KM?
Based on the kinetic constants below, which enzyme will most efficiently catalyze conversion of the substrate into product? A) Vmax = 10 uM s-1, KM = 10 µM B) Vmax = 10 uM s-1, KM = 0.01 µM C) Vmax = 1000 uM s-1, KM = 500 µM D) Vmax = 1 uM s-1, KM = 1 µM E) Vmax = 200 uM s-1, KM = 10 µM
What enzyme kinetic parameters are apparently impacted by competitive inhibitors? Vmax Km Both Km and Vmax Neither Km nor Vmax
You obtain a calculated Vmax of 4.26uM/s and a Km of 122.5uM from a kinetics experiment performed using 0.5uM enzyme. What is the catalytic efficiency of this enzyme?
For an enzymatic reaction, the following data were obtained for two different initial enzyme concentrations: [S](g/L) v ([E0] = 0,015 g/L)(g/L.min) v ([E0] = 0,00875 g/L) (g/L.min) 40 2,28 1,34 20 1,74 1,02 13,4 1,4 0,82 10 1,18 0,68 8 1 0,58 (a)Calculate Vmax (in g/(L.min)) for the initial enzyme concentration equal to 0.015 g/L. (b)Calculate Vmax (in g/(L.min)) for the initial enzyme concentration equal to 0.00875 g/L. (c)Calculate Km (in g/L) for the initial enzyme concentration equal to 0.015 g/L. (d)Calculate Km (in g/L) for the initial enzyme concentration equal to 0.00875 g/L.
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.

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Using linear regression analysis, determine the values of V, and KM of the enzyme in the PRESENCE of max inhibitor: (Express your answer in 3 decimal places, do NOT include the units) V max %3D KM= What is the MODE of inhibition exerted by DEDS?