Use this graph to draw new curves that reflect enzyme activity foreach of the conditions in parts a-c. (Label the curves E + Act, E+Inh, and E-mut.) Then answer part d.a. The enzyme in the presence of a heterotropic allostericactivator (E + Act).b. The enzyme in the presence of a heterotropic allostericinhibitor (E + Inh).c. A mutant enzyme (E-mut) in which the predominant structurein solution consists of monomers that have a higher affinity forthe substrate than that of the tetrameric enzyme.d. Show on the plot how to determine the Km of E-mut. 28. The following graph shows the activity of an enzyme thatfunctions as a homotetramer in which substrate concentration isplotted versus vo/Vmax (ratio of the initial velocity relative to themaximum velocity).Voхешл10.80.60.40.20[Substrate] (mM)

a. The enzyme in the presence of a heterotropic allosteric activator (E + Act).An allosteric…

Answered: Use this graph to draw new curves that…

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

The Ki for a competitive inhibitor pyrrole-2-carboxylate is 0.05M.Calculate the initial velocity if the substrate concentration is 0.25M and 1.0 mole/liter of the inhibitor is added to thereaction.
what concentration of a competitive inhibitor is required to yield 60% inhibition of an enzyme at a substance concentration of 1.0x10^-4 M. The Km for the enzyme is 22 uM and the Ki for the inhibitor is 59 uM. To what concentration must the substrate be increased to reestablish velocity at the uninhibited value?
The table presents the rates of reaction at specific substrateconcentrations for an enzyme that displays classicalMichaelis-Menten kinetics. Two sets of inhibitor data arealso included. Determine the Km and Vmax for the uninhibitedenzyme.
Consider the Michaelis-Menten equation, below: Vmaz (S V. k + [S] %3D What is the relationship between changes in substrate concentration and velocity when the concentration of substrate, [S), is well below k7 The 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 and velocity.
Vmax and Km were calculated for enzyme substrate data. Results Y=0,0063x+0,3929 Km =62,4 mikromol/L Vm =159 mikromol/L.min But two additional data pairs were obtained at low concentrations and new graph equation Y=0,0063x+0,391 Recalculate Vmax and Km and compare and comment with previous results.
Vo 60 50 40 30 20 mm/sec 0100 0 O 0 0 50 100 150 200 250 300 Substrate (mM) Use the Michaelis-Menten plot to answer this question. What is the estimated value of Vmax of the enzyme catalyzed reaction (square data points)? (choose the one best answer) 10
calculate the reaction velocity at saturating substrate concentrations. Your numerical answer is assumed to be in units of M sec-1. [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM
You measure the kinetics of an enzyme as a function of substrate concentration using the Lineweaver-Burke equation. The enzyme concentration is maintained constant at a level of 1 μM. From these data, determine the equation of the line, Vmax, KM, and kcat for the enzyme. [S], μM Velocity, μM/min 2 2.9 3 3.8 4 4.4 5 5.0 6 5.4 7 5.8 8 6.2 9 6.4 10 6.7 The Lineweaver-Burke equation is 1V=1V= __________ (1/|S|) + _________. Therefore, the Vmax is __________ μM/min, KM is ___________ μM, and kcat is ___________ /min.
You measure the kinetics of an enzyme as a function of substrate concentration using the Lineweaver-Burke equation. The enzyme concentration is maintained constant at a level of 1 μM. From these data, determine the equation of the line, Vmax, KM, and kcat for the enzyme. [S], μM Velocity, μM/min 2 2.9 3 3.8 4 4.4 5 5.0 6 5.4 7 5.8 8 6.2 9 6.4 10 6.7 The Lineweaver-Burke equation is 1V=1V= ____________(1[S])(1[S]) + ___________. Therefore, the Vmax is ____________ μM/min, KM is ____________ μM, and kcat is ____________ /min. Round-off all answers to four (4) decimal places.
Please do answer 8.2. 7.1 Is only provided as to understand 8.2.
Solve the Michaelis-Menten equation for KM when vo=Vmax/2. What does this tell you about the relationship between substrate concentration and enzymes with high KM values? With low KM values?
Consider an enzyme-catalyzed reaction that follows Michaelis-Menten kinetics with KM =3.0 mmol·dm-3. What concentration of a competitive inhibitor with KI = 20 umol·dm-3 willreduce the rate of formation of product by 50% when the substrate concentration is held at 0.10mmol·dm-3.

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