4. Using a fluorescent model substrate, you study the kinetics of an enzyme-catalyzed reaction. You observe thebelow data. Write an equation describing reaction velocity (v) versus [S]. Define and provide a numerical value forany constants that you include in your equation.161412420.00.51.01.52.02.53.03.5[S] / mM`N'at 50 mM and observe the followingIn pilot experiments, you add the putative inhibitor imidazoleDoesn't affect anything1reaction velocities:[S] = 1 mM5 µM min-1[S] = 2 mM9 9 µM min-1[S] = 4 mM 911 µM min-1Is imidazole a competitive or non-competitive inhibitor? Provide a brief explanation.>9 00v/ µM min-

Enzymes are the biocatalysts that catalyse the biochemical reactions by lowering the activation…

Answered: 4. Using a fluorescent model substrate,…

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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6. Examine the plot of the enzyme-catalyzed reaction below: Wheat-germ acid phosphatase shows Michaelis-Menten kinetics when acting on para-nitrophenol phosphate 16 14 12 10 8 4 2 0.0 0.5 1.0 1.5 2.0 2.5 3.0 3.5 (S] / mM a) Is this reaction better characterized by Michaelis-Menten kinetics or simple mass action? b) What is the approximate value of Vmax? Km? c) Assuming that this plot was made at 100 nM enzyme, draw the curve, including axis labels, for 300 nM enzyme. d) Imagine that this enzyme is inhibited by a competitive inhibitor with Ki (for inhibitor) = Km (for substrate). Note that v = (kcat [E] tot [S]/Km) / (1 + [S]/Km + [I]/Ki). Draw the curve of reaction velocity (v) versus [S] for [I] = 1 mM. e) Now consider an experiment where you simultaneously introduce substrate and competitive inhibitor at equal concentrations. Make a plot of v versus concentration of [S] = [I], i.e. the X-axis should be the concentration of both I and S, which are equal. v/ uM min-
Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the catalytic efficiency for this reaction. Report your answer in scientific notation to three significant figures in units of M-1s-1.
Consider the two reactions below. They are fast and have reached equilibrium by the end of the time shown. At time zero (t = 0) which is true? [Product] (M) I 2 1 Time The AG of reaction 1 is greater (more positive) than the AG of reaction 2. The AG of reaction 1 is less (more negative) than the AG of reaction 2. ○ The AG of reaction 1 is equal to the AG of reaction 2.
8 7- 6 2- 180 225 270 315 [Substrate] (nM) 45 90 135 360 405 450 495 540 58! What is the KM of the enzyme data shown above? rate (nM/sec) 3.
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Below is kinetic data obtained for an enzyme-catalyzed reaction. The enzyme concentration is fixed at 100 nM. Using a Lineweaver-Burke plot, calculate the kcat value for this reaction. Report your answer to three significant figures in units of 1/sec.
What is the Vmax of an enzyme at 1 μM with -4G RT k = 6.2x 10¹2 s-1 (Ideal gas constant R = 8.314 J K-1 mol-1) cat 0.14 μM S-1 1.4 µM s-1 14 μM s-1 0.14 mM s-1 1.4 mM s-1 activation energy (AG) of 55000 J/mol at 298K?
4. Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium Staphylococcus aureus. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. (8) mg V₂ μmol s1 1.50- 1.25- 1.00- 0.75- 0.50- 0.25- 0.00 0 100 200 300 [s], mM 400 500 WT (a) Estimate the KM and Vmax for the wild-type and mutant enzyme from the graph. V105A (b) Calculate the keat and keat/KM for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.
For an enzyme kinetics experiment, a student prepared a reaction mixture by mixing 450 microliters of 0.75mM PNPP with 4.25ml of 0.2M Tris-HCl buffer. When he is ready to measure the absorbance, he added 0.3ml of Alkaline Phosphatase to the mixture and mixed thoroughly. What is the substrate concentration at the beginning of the reaction in mM ?
2. Enzyme-catalyzed reactions. Answer the following with true or false. If false, explain why. (a) The initial rate of an enzyme-catalyzed reaction is independent of substrate concentration. (b) At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. (c) The Michaelis constant Km equals the substrate concentration at which velocity (v) = Vmax/2. (d) The Km for a regulatory enzyme varies with enzyme concentration. (e) If enough substrate is added, the normal Vmax of an enzyme-catalyzed reaction can be attained even in the presence of a noncompetitive inhibitor. (f) The Km of some enzymes may be altered by the presence of metabolites structurally unrelated to the substrate. (g) The rate of an enzyme-catalyzed reaction in the presence of a rate-limiting concentration of substrate decreases with time. (h) The sigmoidal shape of the v versus [S] curve for some regulatory enzymes indicates that affinity of the enzyme for the…
3. Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium Staphylococcus aureus. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. -1 v, μmol s¹ mg-¹ 1.50- 1.25- 1.00- 0.75- 0.50- 0.25- 0.00+ 0 100 → WT 200 300 [s], mM 400 500 → V105A (a) Estimate the Km and Vmax for the wild-type and mutant enzyme from the graph. (b) Calculate the Keat and Keat/Km for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.
You run a series of assays at 25°C on enzyme A. You measure the velocity for a range of S concentrations. What is the Km (in mM) for Enzyme A?

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