Consider the Michaelis-Menten equation, below:Vmaz (SV.k + [S]%3DWhat is the relationship between changes in substrate concentration and velocity when the concentration of substrate, [S), is well below k7The S terms cancel out in this equation, so there is no effect of changing substrate concentration.The S] term in the numerator is negligible, so there is no impact of changing substrate concentration.Because the enzyme has reached Vr there is no effect of changing substrate concentrations on enzyme velocity.OThe [S term in the denominator is negligible compared to k There is a linear relationship between substrate concentration andvelocity.

[S] : Substrate concentration V= Vmax[S]/(Km+[S]) Vmax: Maximum velocity Km: [S] at which V is…

Answered: Consider the Michaelis-Menten equation,…

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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The above graphs (Lineweaver-Burk) were plotted using data from an experiment that investigated changes in initial velocity, V0, (in mmol/min) as a function of substrate concentration, [S], (in mmol/L) for an enzyme-catalysed reaction. The initial velocity was measured at a fixed concentration of enzyme at different concentrations of substrate in the absence of any inhibitor and was then repeated in the presence of a competitive inhibitor at two different concentrations. Use the graph to determine the maximal velocity of the reaction the Km value of the uninhibited reaction the Km value of the reaction with (i) the lower level of inhibitor and (ii) the higher level of the inhibitor. TEMPLATE FOR ANSWERS Vmax of uninhibited reaction Intercept on y-axis = = __________________ Vmax = __________________ Km value of the uninhibited reaction Intercept on x-axis = =…
when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.
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
For an enzyme that obeys Michaelis-Menten kinetics, in order for the reaction velocity (v) to be 80% of the maximal velocity (Vmax), the substrate concentration must be…. Choice 1 of 5:½ Km Choice 2 of 5:2 Km Choice 3 of 5:4 Km Choice 4 of 5:8 Km Choice 5 of 5:not enough information is given
. Lineweaver-Burk plot is the most used linearization method of the MichaelisMenten equation, but the main drawback is a/an:a. overemphasis to low substrate concentration and less emphasis to high substrate concentration.b. overemphasis to high substrate concentration and less emphasis to low substrate concentration.c. exaggeration to both ends of the reciprocal of the substrate concentration.d. lack of independent variables to x- and y- coordinates.Kinetic data were gathered for Enzyme X, its substrate, and a known competitive inhibitor Z. Upon plotting the linearized kinetic data, one could surmise that the plot of the inhibited enzyme would have:a. a slope and y-intercept both lower in magnitude than the plot of the uninhibited enzyme using Eadie-Hofstee method.b. a constant slope and y-intercept that is lower in magnitude with the plot of the uninhibited enzyme using Eadie-Hofstee method.c. a slope and y-intercept greater in magnitude than the plot of the uninhibited enzyme using…
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.
assume that for an enzyme immobilized on the surface of a nonporous support material, the external mass-transfer resisitance for substrate is not negligible as compared to the reaction rate.The enzyme is subject to substrate inhibition are multiple states possible?why or why not? could the effectiveness factor be greater than one?
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.
Use the relationships revealed by a Lineweaver–Burk plot and the table of enzyme performance to calculate the ?max and ?M of the enzyme with no inhibitor, with inhibitor A, and with inhibitor B. Substrate concentration, [S], has units of micromolar, μM. Enzyme velocity, ?0, has units of micromole per minute, (μmol/min). Using data from only the extremes of the [S] range is unreliable. Select the type of inhibition displayed by inhibitor A. competitive noncompetitive uncompetitive Select the type of inhibition displayed by inhibitor B. competitive noncompetitive uncompetitive

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