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…

Answered: 1. In the Lineweaver-Burk plots shown…

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 graphs 3 and 4 representing 1/Vo = f(1/[S]o) have been done in the presence of a competitive (CI) and noncompetitive inhibitor (NCI). a- For each figure, determine from the relative position of the straight lines which one is obtained in presence of an inhibitor. b- Indicate which graph corresponds to the competitive inhibition and which one the noncompetitive inhibition. Justify your answer. c- Complete the graphs by indicating which values can be determined from the arrows. 3 1/No 1/[S]⁰ (4) 1/No 1/[S]o
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
The following data, presented by G. Bowes and W. L. Ogre in J. Biol. Chem. (1972) 247:2171-2176, describe the relative rates of incorporation of CO, by Rubisco under N, and under pure Oz. Decide whether Oz is a competitive or uncompetitive inhibitor. [CO] (mM) Under N2 Under O2 0.20 16.7 10 0.10 12.5 5.6 0.067 8.3 4.2 0.050 7.1 3.2
Using the attachment, Answer the following questions: Prepare a double reciprocal plot with all three experiments (lines) on the same graph. Use your graph, and then answer items 2, 3, and 4 below. 1. Calculate the Vmax or apparent Vmax for all three sets of data. Likewise, calculate the Km or apparent Km for each set. 2. For Inhibitor X, what is the mode/type of inhibition? 3. For Inhibitor Z, what is the mode/type of inhibition? By comparison of the apparent Vmax to the control Vmax, what is the value of α’, as defined in class? If Ki’ = 10 mM for this inhibitor, then what must the inhibitor concentration [Z] be?
1. The antibacterial activity of flavonoids was tested against the bacterial strain, Escherichia coli. The minimum inhibitory concentration at which 50% of the compounds were inhibited (MIC50) are presented in the table below for some of the compounds. Table 1: Antibacterial activity of flavonoids tested against E. coli Compound MIC50 (µg/mL) Kaempferol 25.50 Quercetin 35.76 36.72 67.25 137.10 156.34 238.94 320.88 Compound X Luteolin Tangeritin 5,6,7,4'-Tetramethoxyflavone Genistin Genistein 1.4 If galangin were tested, how would its antibacterial activity compare to that of the other flavonoids? Explain your answer.
The figure below shows the dependence of the enzyme's rate, v (in µM/min), as a function of substrate concentration, S (in mM). Also shown is the dependence of the rate in the presence of an inhibitor, present at a concentration of 0.2 mM. Based on this information, which of the following does this inhibitor most likely interact with? 1/v 1- 05 1/[S) O A. Michaelis complex O B. [E O C. free enzyme O D. free substrate O E. Both "A" and "B."
. The following data, presented by G. Bowes and W. L. Ogre in J. Biol. Chem. (1972) 247:2171–2176, describe the relative rates of incorpo- ration of CO, by rubisco under N, and under pure O,. Decide whether O, is a competitive or uncompetitive inhibitor. [CO,] (mM) Under N2 Under O, 0.20 16.7 10 0.10 12.5 5.6 0.067 8.3 4.2 0.050 7.1 3.2
1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?
A schematic representation of the enzyme IspD complexed to inhibitor 3, and a series of inhibitors 3-5 are shown below. Ala202 lle240 mwww NH NH Val263 ОН www HN N- lle177 HN 'N' CI 3 X = N 4 X = C-CN 5 X = C-COO IC50 274 µM IC50 140 nM IC50 35 nM NH2 HN Val266 N -N O-H---- N HN %3D Arg157 HN wwww lle265 Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why structure 5 is a much weaker inhibitor (higher IC50 value) than 3 and 4.
Match the different names for inhibition mechanisms (1-5) with a description of their properties 7a-7d: 1. competitive inhibitor. 2. allosteric inhibitor also known as non-competitive inhibitor. 3. un-competitive inhibitor. 4. affinity label also known as active site directed covalent (irreversible) enzyme inhibitor. 5. Kcat inhibitor, also known as a mechanism-based covalent (irreversible) enzyme inhibitor. 4a. An enzyme inhibitor in which a substrate or competitive inhibitor is modified so that it contains a chemically reactive electrophile which can bind to and subsequently react with the enzyme active site: 4b. An enzyme inhibitor that contains latent reactive group that upon binding followed by catalytic turnover at the enzyme active site produces a reactive electrophile that reacts covalently with the enzyme: 4c. A reversible inhibitor that competes with the substrate for binding to the enzyme active site: 4d. A reversible inhibitor that can bind independently of substrate to its…
Data from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these values with assays run without inhibitor are used to understand how the inhibition is occurring. This is useful for better understanding the active site as well as the practical aspect of pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of inhibitors. Comnetitive Uncomnetitive Mixed +Inh +Inh 4Inh Anh Inh Anh [S] [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed c. For each situation in Model 1, consider an inhibitor that is better than the one shown on the graph. Answer the following questions for each type of inhibition: i. How would the KmPP change? ii. How would the Vmax PP change?
You were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newly discovered enzyme known as BILISTASE. The kinetics data are shown below: [Substrate, µM] Vo with DEDS (µM/min) Vo without DEDS (uM/min) 1.667 1.600 3.544 12.500 1.923 4.259 13.333 2.139 4.737 %3D 14.000 2.268 5.019 5.000 2.410 5.336 Using linear regression analysis, determine the values of Vmax and KM of the enzyme in the ABSENCE of inhibitor: (Express your answer in 3 decimal places, do NOT include the units) Vmax = KM=

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