In an enzyme kinetics study, three inhibitors resulted to the following results:Inhibitor ABCInhibitor XYZ Inhibitor PQR Without InhibitorV40.2 mM/sec40.3 mM/sec12.32 mM/sec65.43 mM/secmaxK24.3 mM28.5 mM24.3 mM15.7 mMc. The inhibition occurred at 37.0o°c. Assuming that the temperature increased to37.5°c, what will happen to the VXYZ? Why do you say so? Provide illustrations using appropriate dimensions in the xand K in the chemical system involving inhibitormaxand y axes.

The rate of a enzyme catalyzed reaction increases with temperature until a point and once the…

Answered: In an enzyme kinetics study, three…

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

For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s -1 , k-1 = 3.1 ⅹ 104 s -1 , and k2 = 3.4 ⅹ 105 s -1 . a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach rapid equilibrium or the steady state? Show work justify b) What is kcat for this reaction? Show work justify c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1 , and each enzyme has two active sites.
From your Lineweaver-Burk plot,the vlaues are: Km Vmax Uninhibited 0.09 mmol/L 3.02 min/mmol Inhibited 6.22 mmol/L 9.98 min/mmol By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.
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.
At body temperature (37°C), k of an enzyme-catalyzed reaction is 2.3X10¹⁴ times greater than k of the uncatalyzed reaction. Assuming that the frequency factor A is the same for both reactions, by how much does the enzyme lower the Eₐ?
The following kinetic data were obtained for an enzyme in the absence of an inhibitor (1) and in the presence of two different inhibitors (2) and (3) at 5mM concentration. [S], mM (mmol/mL/sec) (mmol/mL/sec) (mmol/mL/sec) (1) (2) (3) 1 12 4.3 5.5 2 20 8 9 3 29 14 13 8 35 21 16 12 40 26 18 Determine the Vmax and KM of the enzyme Determine the type of inhibition.
Under the following conditions, fill in the blanks. Then, describe why this inhibitor is the type of inhibitor you identified it as. If you were to add 5nM of a reversible inhibitor, the Km for the measured enzyme catalyzed reaction would ______ (Increase, Decrease, Stay the same) to ______µM (choose appropriate value) and Vmax would _______ (Increase, Decrease, Stay the same) to ______µMs-1. So, this inhibitor is a ______ (Competitive, Uncompetitive, Mixed) inhibitor. Conditions: kcat = 130 s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µM
A particular enzyme-catalyzed reaction has an apparent Vmax = 9.00 nmol s-1 and α' = 3.00 when 2.00 µmol L-1 inhibitor X is present and uncompetitively inhibiting the reaction. Calculate Vmax for the uninhibited reaction in nmol s-1.
At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?
List 4 major types of inhibition modes and clearly indicate the effect on Vmax and KM for each mode?2. What is the effect of each of the 4 types of inhibitors on the initial rate of an enzyme catalyzed reaction?3. A potent inhibitor effectively inhibits an enzyme catalyzed reaction. What kind of a Ki value you would expect for a potent inhibitor?4. Considering PNPP → PNP reaction, would you expect to see more intense or pale color for the reaction that contain the inhibitor? Explain.
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).

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