True/False Question: The double-reciprocal transformation of the Michaelis-Menten plot, also called the Lineweaver-Burk plot, is used to solve (graphically) for the rate of an enzymatic reaction at infinite substrate concentration, which is impossible to achieve experimentally. O True O False
Q: True/False Question: Enzymes perform catalysis by selectively increasing the rates of the forward…
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A: Background information Km is that substrate concentration at which velocity is half of the maximum.…
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A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation energy…
Q: Explain why each of the following data sets from a Lineweaver–Burk plot are not individually ideal…
A: Lineweaver-Burk plot is the graphical representation of Lineweaver-Burk equation which is a double…
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A: The equilibrium constant of a chemical reaction is the value of its reaction quotient at chemical…
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A: From the LB plot of enzyme kinetics, y=mx+c It's an equation of a straight line. 1/V=(Km/Vm )1/S…
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A: Note: We are authorized to answer one question at a time since you have not mentioned which question…
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A: The rate of reaction is expressed in terms of change in the concentration of a reactant or product.…
Q: [Substrate, uM] Vo with DEDS (µM/min) Vo without DEDS (µM/min) 3.333 0.774 1.196 4.000 0.877 1.316…
A: Given data of interest (X, Y) values where X denotes the substrate concentration in uM and Vo…
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A: Lineweaver-Burk plot, also known as double-reciprocal plot, is the graph plotted for Lineweaver-Burk…
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A: Michaelis menten constant, Km is the substrate concentration required to produce half maximum…
Q: columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in…
A: Michaelis Menton equation relates velocity of enzymatic reaction with substrate…
Q: Question 1 What type of a relation do we expect to get if we fix the enzyme concentration and look…
A: Hi! Thanks for your question. As you have posted multiple questions and have not mentioned which one…
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Q: QUESTION 2 The Michaelis-Menten and the Lineweaver-Burk plots can be used to determine the Km and…
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Q: QUESTION 17 calculate the KM AND the total amount of enzyme present in these experiments. The…
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Q: Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any…
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Q: True/False Question: Side chain of a serine residue in the active site of an enzyme can serve as a…
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A: Enzymes are catalysts that enhance the rate of biochemical reactions.
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A: Given, For experiment 1 [I] [S] Vo 1/S 1/Vo 0 mM 0.1 mM 0.33 10 3.03 0 mM 0.2 mM 0.50 5 2…
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Q: Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any…
A: Given Values: Line (A) y-intercept = 0.3 secμM Slope of Line (A) = 1.8 sec Enzyme concentration used…
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Q: What is the Vmax of this enzyme WITHOUT inhibitor? Please show your work. b. What is the Km of…
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Q: Consider two enzymes A and B, which are not related. However, the two enzymes coincidentally share…
A: Consider two enzymes A and B, which are not related. However, the two enzymes coincidentally share…
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Q: QUESTION 1 What TYPE of inhibition is observed in the following plot: V KK [S], mM m Competitive…
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- Question 2. Answer the following questions: A. The following experimental data was collected during a study of the catalytic activity of anintestinal peptidase with the substrate glycylglycine. Plot the data as a graph, and use it toestimate the Km and the Vmax for this enzyme. B. Now transform this data to plot it as a straight line (Lineweaver-Burk plot). Determine Km andthe Vmax for this enzyme using this new plot. Do your results agree with the estimates made fromthe first graph of the raw data (from 2A)? C. Now assume that the activity of this intestinal peptidase is regulated by covalent modificationof its catalytically active amino acid. Upon phosphorylation, the Km of the catalyzed reaction has been observed to increase by a factor of 3 without any effect on its Vmax. Is the enzyme getting activated or inhibited upon phosphorylation? Justify your answer. D. How will the Lineweaver-Burk plot of the phosphorylated enzyme differ from the plot of the unmodified enzyme (from 2B)?…The comparison of the active site geometries of chymotrypsin and subtilisin under the assumption that their similarities have catalytic signifi cance has led to greater mechanistic understanding of both these enzymes. Discuss the validity of this strategy.Mechanisms of catalysis : 2.1 Acid-base catalysis summary + example 2.2 Electrostatic catalysis summary + example 2.3 Covalent catalysis summary + example 2.4 Enzymen catalysis summary 2.5 Mechanism of chymotrypsin summary. These mechanisms involve several of the above-mentioned catalyses. In these summaries, do not just draw a diagram of the proposed mechanisms. It is more important to understand which reaction steps involve what kind of catalysis and how these help to reduce the activation energy needed for the reaction (e.g. a step in the reaction mechanism could be electrostatic catalysis to stabilise the transitions state) 2.6 Mechanism of lysozyme summary. These mechanisms involve several of the above-mentioned catalyses. In these summaries, do not just draw a diagram of the proposed mechanisms. It is more important to understand which reaction steps involve what kind of catalysis and how these help to reduce the activation energy needed for the reaction (e.g.…
- 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 Km of the reaction represented by Line (B).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. Line (B) 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.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. 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)…
- Catalase is the enzyme. experiment with h2O2 3. What is the marker for the enzyme’s optimum condition?The Lineweaver-Burk plot, which illustrates the reciprocal of the reaction rate (1/v) versus the reciprocal of the substrate concentration (1/[S]), is a graphical representation of enzyme kinetics. This plot is typically used to determine the maximum rate, Vmax, and the Michaelis constant, Km, which can be gleaned from the intercepts and slope. Identify each intercept and the slope in terms of the constants Vmax and Km. What term is represented by C? Linewegver-Burk Pt 1/Vmax O A. В. -1/Km Km/Vmax C.Intracellular and extracellular enzymes require different extraction methods. Provide 2 examples of intracellular enzyme extraction methods and explain the reason for performing this step.