1. In the Lineweaver-Burk plots shown below, In the Lineweaver-Burk plots shown below, oneof the lines represents data collected for an enzyme in the absence of an inhibitor. A secondline represents data collected for the same enzyme in the presence of a competitiveinhibitor. Finally, a third line represents data collected for the same enzyme in the presenceof a noncompetitive inhibitor. Which of the following is the best identification of the threelines? Which of the following is the best identification of the three lines?0.6 -0.4 -0.2 a.0 02 04 06 ON 10 121/Line Y ()Noncompetitive inhibitorLine X (*)Line Z (o)A. Competitive inhibitorNo inhibitorB. Competitive inhibitorNo inhibitor inhibitor|Noncompetitive inhibitorC. No inhibitorNoncompetitive inhibitorCompetitive inhibitorD. No inhibitorCompetitive inhibitorNoncompetitive inhibitorState if the following is True or False:1. The occurrence of ionic interactions between water molecules gives liquid water a regularthree-dimensional structure.2. The infectious prion protein which are believed to cause a neurodegenerative disease byacting as a template to misfold other cellular prion proteins are usually B-helices.

The plot of reciprocal of V and S is known as Lineweaver-Burk plot (LB plot) or double reciprocal…

1. In the Lineweaver-Burk plots shown below, In the Lineweaver-Burk plots shown below, one of the lines represents data collected for an enzyme in the absence of an inhibitor. A second line represents data collected for the same enzyme in the presence of a competitive inhibitor. Finally, a third line represents data collected for the same enzyme in the presence of a noncompetitive inhibitor. Which of the following is the best identification of the three lines? Which of the following is the best identification of the three lines? 0.6 -0.4 -0.2 a0 02 04 06 Os 10 12 1/N Line X (*) A. Competitive inhibitor Line Y () Noncompetitive inhibitor Line Z (0) No inhibitor B. Competitive inhibitor No inhibitor inhibitor Noncompetitive inhibitor

1. In the Lineweaver-Burk plots shown below, In the Lineweaver-Burk plots shown below, one of the lines represents data collected for an enzyme in the absence of an inhibitor. A second line represents data collected for the same enzyme in the presence of a competitive inhibitor. Finally, a third line represents data collected for the same enzyme in the presence of a noncompetitive inhibitor. Which of the following is the best identification of the three lines? Which of the following is the best identification of the three lines? 0.6 -0.4 -0.2 a0 02 04 06 Os 10 12 1/N Line X (*) A. Competitive inhibitor Line Y () Noncompetitive inhibitor Line Z (0) No inhibitor B. Competitive inhibitor No inhibitor inhibitor Noncompetitive inhibitor

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 9TYK: Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric...

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A biochemst wants to dtermine the effect of inhibitor on a certain enzyme. See attached data. Using linaer regression analysis, determine the values of Vmax and Km of the enzyme in the absence of an inhibitor 1. y- int ( up to 5 decimal places) 2. slope 3. Vmax 4. Km Using linear regression analysis determine the values of Vmax and Km of the enzyme in the presence of inhibitor 1. y- int ( up to 5 decimal places) 2. slope 3. Vmax 4. Km
2. an enzyme-catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained. (S)[M] V (umol/min) V (+inhibitor)(umol/min) 6 x 10-6 20.8 12 1 x 10-5 29 15 2 x 10-5 45 20 6 x 10-5 67.6 24 1.8 x 10-4 87 28 plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots. calculate the Km of enzyme in the reaction without inhibitor Km1 of the enzyme in the reaction with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction what kind of inhibitor was added to the enzyme-catalyzed reaction? explain your answer in terms of changes in Km and Vmax.
What is the kinetical hallmark of reversible competitive inhibition? A. Vmax cannot be attained, even at high substrate concentrations. B. Vmax can be attained at sufficiently high concentrations of substrate. C. The apparent value for KM decreases as more inhibitor is added. D. The apparent value for KM remains unchanged as more inhibitor is added. E. Vmax decreases as more inhibitor is added.
Which of the following statements about inhibition is true? a. Allosteric inhibitors and allosteric activators are competitive for a given enzyme. b. If an inhibitor binds the active site, it is considered noncompetitive. c. If an inhibitor binds to a site other than the active site, this competitive inhibition. d. A noncompetitive inhibitor is believed to change the shape of the enzyme, making its active site inoperable. e. Competitive inhibition is usually not reversible.
Indicate whether each of the following statements describes a reversible competitive inhibitor, a reversible noncompetitive inhibitor, or an irreversible inhibitor. More than one answer may apply.a. Both inhibitor and substrate bind at the active site on a random basis.b. The inhibitor effect cannot be reversed by the addition of more substrate.c. Inhibitor structure does not have to resemble substrate structure.d. The inhibitor and substrate can bind to the enzyme simultaneously
1. A. Estimate from the graph what the Vmax is for the enzyme without inhibitor present (black circles) and in the presence of the inhibitor (green squares). B. Estimate the Km from the graph without inhibitor present (black circles) and in the presence of the inhibitor (green squares). C. Based on the data, what type of reversible inhibitor do you think was used? Explain your answer.
Inhibitor X exerts which of the following effects on the above enzyme (lactase)? (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) pure non-competitive inhibition uncompetitive inhibition competitive inhibition all of the above none of the above
For competitive inhibition: a. the value of Km decreases b. the value of Vmax decreases c. it is possible to overcome the effect of the inhibitor by increasing the concentration of substrate d. none of the above
Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and Km of the enzyme with no inhibitor. with inhibitor A, and with inhibitor B. [S] (uM) Vo (umol/min); w/ no inhib. Vo (umol/min); w/ inhib. A Vo (umol/min); w/ inhib. B 10 6.3 5.1 4.0 40 18.4 15.8 11.8 100 29.9 27.0 19.1 150 34.7 32.0 22.2 No inhib. Vmax= Km= Inhib. A Vmax= Km= Inhib. B Vmax= Km=
A noncompetitive inhibition can be overcome/reverse by which of the following: a. Increasing [enzyme] b. Increasing [Substrate] c. Increasing [product] d. All of the above
1. How much faster is a reaction with the faster enzyme than without a catalyst? * A. Approximately 10 times faster. B. About 100 times faster. C. Approximately 1,000 times faster. D. About 10,000 times faster. E. About 10X^20 times faster. 2. For competitive inhibition * A. KM value decreases B. the value of Vmax decreases C. it is possible to overcome the effect of the inhibitor by increasing the concentration of substrate D. None of the above
Under what conditions does Km represent the true binding affinity (i.e. Kd) of the substrate to the enzyme? 1. when kcat << k-1 2. when k-1 >> k1 3. when k1 >> kcat 4. when k1 = k-1