UYou record and plot the kinetics of an allosteric enzyme in three experiments. First, youmeasure kinetics with only enzyme and substrate (black line). Then you measure kinetics withenzyme, substrate, and compound 1 (blue line), and finally, with enzyme, substrate, andcompound 2 (orange line). Which of the following are true? (Pick two.)Vmax1[S]2Compound 1 is an allosteric activator.Compound 1 is an allosteric inhibitor.Compound 2 is an allosteric activator.Compound 2 is an allosteric inhibitor.

Important Terms: Allosteric EnzymesAllosteric enzymes are proteins that change their conformation…

Answered: U You record and plot the kinetics of…

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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How many of the following statements are true? Allosteric enzymes display sigmoidal kinetics for plots of V versus [S] Allosteric enzymes exist in T and R states Allosteric enzymes display kinetics that becomes less sigmoidal in the presence of activators
5. By using Excel or GoogleSheets. graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Kwax values for the inhibited and uninhibited reactions? Is the inhibitor competitive or noncompetitive? [S] (mM) V, No Inhibitor (mmol min-) V, Inhibitor Present (mmol min-') 1 × 10-4 5 × 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 0.026 0.010 0.092 0.136 0.040 0.086 0.150 0.120 0.165 0.142
5. 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 equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop a
Can you please help solve this problem?
MAKE A GRAPH FOR ME ON GRAPH PAPER CALL IT ENZYMES VS RATE OF REACTION USING TABLE BELOW GRAPH paper INSERTED BELOW rules: data points must be an x or circled dot, must be on grid paper , the independant variable on the x axis and dependant variable on the y axis, must include titles Regarding the data points: - H2O2 + MnO2 Control #1: (Control #1, 5)- H2O2 + sand control #2: (Control #2, 0)- Plant versus Animal Liver Catalase: (Liver, 4)- Potato: Plant vs. Animal Catalase: (Potato, 3)- Substance Enzyme Concentration (Used Liver): (Liver Used, 4)- Substance Enzyme Concentration (Used H2O2): (Used H2O2, 1) - Boiling Water Bath Temperature: (Boiling Water Bath, 5)- Ice Water Bath Temperature: (Ice Water Bath, 2)- HCl, or pH 3: (H 3, 4)- NaOH at pH 12: (pH 12, 2)- pH 7 (H2O): (assuming average of pH readings; pH 7, not specified) The following explains how to display the graph: Title: Factors versus Enzyme Activity Rate - Labels on X- and Y-axes: Factors and Rate of Enzyme…
Explain how the observation that reaction (B) runs faster than reaction (A) is related to the enzyme catalysis.
An enzyme contains an active site aspartic acid with a pKa = 5.0, whichacts as a general acid catalyst. On the accompanying template, draw thecurve of enzyme activity (reaction rate) versus pH for the enzyme (assumethat the protein is stably folded between pH 2–12 and that the active siteAsp is the only ionizable residue involved in catalysis). Briefly explain theshape of your curve.
4. Using a fluorescent model substrate, you study the kinetics of an enzyme-catalyzed reaction. You observe the below data. Write an equation describing reaction velocity (v) versus [S]. Define and provide a numerical value for any constants that you include in your equation. 16 14 12 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 [S] / mM `N' at 50 mM and observe the following In pilot experiments, you add the putative inhibitor imidazole Doesn't affect anything 1 reaction velocities: [S] = 1 mM5 µM min-1 [S] = 2 mM9 9 µM min-1 [S] = 4 mM 911 µM min-1 Is imidazole a competitive or non-competitive inhibitor? Provide a brief explanation. > 9 00 v/ µM min-

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