**Transcription for Educational Use**23. The drug UTSAone was investigated as a possible inhibitor of a dehydrogenase enzyme that acts on pregnenolone as a substrate in steroid synthesis. The activity of the dehydrogenase was measured in the presence and in the absence of 10 μM UTSAone. Use the data in the table to construct a Lineweaver-Burk plot.| [Pregnenolone, μM] | v₀ without I (pmol/min) | v₀ with I (pmol/min) ||---------------------|-------------------------|----------------------|| 1.0 | 0.00106 | 0.00079 || 5.0 | 0.00327 | 0.00242 || 10.0 | 0.00439 | 0.00326 || 20.0 | 0.00529 | 0.00395 |**Which of the following statements are TRUE?**A. The Kₘ (μM) in the absence of UTSAone is 2.4. B. The Kₘ (μM) in the absence of UTSAone is 5.4. C. The Kₘ (μM) in the presence of UTSAone is 2.4. D. The Kₘ (μM) in the presence of UTSAone is 5.3. E. The Vmax (pmol/min) in the absence of UTSAone is 6.8 x 10⁻³. F. The Vmax (pmol/min) in the presence of UTSAone is 5.0 x 10⁻³. G. The x-intercept (μM⁻¹) in the absence of UTSAone is -0.186. H. The x-intercept (μM⁻¹) in the presence of UTSAone is -0.188. I. UTSAone binds to a site other than the active site on the dehydrogenase.**Explanation:**The table provides data on the reaction rates (v₀) with varying concentrations of the substrate (pregnenolone) both in the absence and presence of the inhibitor (UTSAone). This data is used to create a Linewe

Enzyme-Substrate-Inhibitor interactions that obey the Michaelis Menten Kinetics show unique…

Answered: 23. The drug UTSAone was investigated…

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 enzyme triosephosphate isomerase (TIM) catalyzes the following reaction in glycolysis, where it converts dihydroxyacetone phosphate (DHAP) to glyceraldehyde-3-phosphate (GAP). CH₂OH C=O CH₂OPO²- DHAP triose phosphate isomerase [DHAP] (MM 1.00 2.00 3.00 6.00 O V. (mM/s) 3.700 6.727 9.250 14.800 = H HCOH CH₂OPO²- Kinetics experiments were performed on TIM. Enzyme activity (initial velocity, V.) was measured at varying concentrations of DHAP. The enzyme kinetics were also measured in the presence of two inhibitors, A and B. The enzyme concentration used in all experiments was 25.00 μM. The data are shown below. GAP V. (mM/s) + A 1.452 2.794 4.038 7.281 V₁ (mM/s) + B 0.755 1.379 1.905 3.077
ver is given. A +B C+ D 1) Calculate AG for the above react un and indicáte whether the reaction is favorable or unfavorable [A] = 0.9 M 20°C AG° = 4 KJ/mol %3D [B] = 15mM [C] = 4mM [D] = 3 M R= 8.314 J/moleK %3D %3D 4.7 and explain how you know.
Acetazolamide is a drug which inhibits carbonic anhydrase. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. Figure 2 shows the experimental curve of initial reaction velocity (as percentage of Vma) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor 50 Acetazolamide 0.2 0.4 0.6 0.8 [S] (mM) Figure 2 (i) Compare the maximal velocities and Michaelis Menten constants of the enzyme in the absence and the presence of the inhibitor acetazolamide. Determine the nature of inhibition by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide. Sketch a graph of V versus [S] showing curves in the absence of an inhibitor and in the presence of the types of inhibitors not shown by acetazolamide. ("AJO %) A
For an enzyme following Michaelis-Menten kinetics, the following Vo vs. S data were obtained in steady state experiments using 2 micromolar enzyme for all measurements: [S] Vo 1 mM 4.0 mM/min 2 mM 4.8 mM/min 4 mM 4.9 mm/min 8 mM 4.95 mM/min Estimate the value of kcat for the reaction. Be sure to include the appropriate units.
8L.3.4
Phosphoglycerate-mutase catalyses the isomerization of 3-phospho-glycerate to 2-phospho-glycerate. The enzyme has a molecular weight of 28,556 g/mol. In assays using 1 milligram of enzyme per assay the Km for 3-phosphoglycerate was 1.2 x 10^-3M and the Vmax was 840 μmole min^-1. What would be the Vmax in units of mole s^-1?
80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
Paper electrophoresis of Asn, Ala, Asp, Lys and Ser mixtures at pH = 7 shows the fastest movement towards the anode The fully saponified 10g oil sample consumed 1.87g KOH, and the iodine value of the oil was 28.3. So how many unsaturated double bonds are there in each oil molecule on average? (lodine is known to have an atomic weight of 127) Given that 100g cellulose sample is completely hydrolyzed to obtain 78g glucose, then the percentage of cellulose in the sample is _% Given that the Km of catalase is 20mmol/L and the substrate concentration is 80mmol/L, then the percentage of catalase bound to the substrate is %
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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.
Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
Determine the minimum inhibitory concentrations (MIC) for compounds 1, 2, and 3 based on the microdilution results.

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