2. If the enzyme maltase has a V of 2.0 mM per minute when [S] = 0.50 mM, and a V of 5.0 mM per 0 minute when [S] =2.0 mM, what is its V? max A. 0.20 mM per minute B. 0.50 mM per minute C. 1.0 mM per minute D. 2.0 mM per minute E. 10.0 mM per minute
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- 2. Two different enzymes are able to catalyze the same reaction, A→ B. They both have the same Vmax, but differ in their Km for the substrate A. For enzyme 1, the Km is 1.0 mM; for enzyme 2, the Km is 10 mM. When enzyme 1 was incubated with 0.1 mM A, it was observed that B was produced at a rate of 0.0020 mmoles/minute. a. What is the value of the Vmax of the enzymes? b. What will be the rate of production of B when enzyme 2 is incubated with 0.1 mM A? C. What will be the rate of production of B when enzyme 1 is incubated with 1 M (i.e., 1000 mM) A? d. Which enzyme is a more efficient catalyst?3. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the following data were obtained: [S] (M) 2.5 x 10-6 4.0 x 106 1х 105 2 x 105 4х 10-5 1 x 104 2 x 10-3 1 x 102 Vo (µM / min) 28 40 70 95 112 128 139 140 A. Vmax = 140 and Km=1 x 10-5 B. Vmax = 70 and Km = 1 x 103 C. Vmax = 140 and Km=1 x 10-2 D. Vmax = 70 and Km = 1 x 10-² %3D1. Enzyme X has a molecular weight of 35,000 Da. When this enzyme is assayed for enzyme activity, the corresponding line of the double reciprocal plot has the equation y = 75,253X + 102,392. The substrate concentration was in mM and the velocity was measured in mM min". From these data calculate the following: a. KM and Vmax b. kcat if the enzyme concentration was 2 mg/mL. 2. When you run enzyme X from question one on an SDS-PAGE you find that, after Coomassie staining, there is only one band on the gel that runs just below the 20,000 Dalton molecular weight marker. What does this result tell you about the nature of the quaternary structure of your enzyme?
- 1. How much 1 M citrate would you need to make 100 mL of 0.5 M citrate? Give the answer in ug/ul 2.If you added 59 grams of Succinate MW=118.1 to 1 L of H2O, what would be the resulting concentrations (in M) of succinate in that solution? 3. What is the volume of a cell that has a diameter of 6 um?0.0025 0.002 0.0015 0.001 0.0005 10 20 30 40 50 60 70 80 -0.0005 Temperature (C) 1.What trend did you observe for the rate of peroxidase compared to the temperature of the enzyme? 2.What was the optimum temperature tested for the enzyme peroxidase? 3.Did any of the temperatures tested cause the enzyme to denature? Which one? Rate (abs/sec @ 500nm)2. A 500µl reaction containing 0.5 pmol of an enzyme following Michaelis -Menten kinetics with saturating substrate concentration is studied. For this enzyme kl = 1 x 10° M-1 s', k-1 = 2 x 10's', and k2 = 1 x 10° s'. a. What is the Vmax for the enzyme considering that it has only one substrate binding site? b. What are the values of Km and Ks? Is this a rapid equilibrium enzyme or does it follow steady state kinetics? Explain why. c. What is the substrate concentration needed to achieve half maximal velocity? Explain the basis for your answer. d. If the substrate concentration in part e is doubled, how many fold will the initial velocity increase? e. What is the Km is the concentration of the enzyme is doubled? f. What is the efficiency of this enzyme? g. Would this enzyme be considered a perfect enzyme? Explain. h. If 0.25 pmol of an irreversible or classic non-competitive inhibitor is added before starting the reaction. What is the resulting Km for the enzyme? i. A reversible…
- 3. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the following data were obtained: [S] (M) Vo (uM / min) 2.5 x 106 4.0 x 106 28 40 1 x 105 2 x 105 4 x 105 1 x 104 2х 103 1x 10-2 70 95 112 128 139 140 A. Vmax = 140 and Km =1 x 10s B. Vmax = 70 and Km = 1 x 105 C. Vmax = 140 and Km =1 x 102 D. Vmax = 70 and Km = 1 x 102 %3D %3!4. How much lactic acid (C3H6O3) is produced when 225 g glucose (C6H1206) is used as substrate in the fermentation. Assuming that the sugar is completely fermented to lactic acid. The molar masses of CsH12O6 and C3HGO3 are 180.156 g/mol and 90.08 g/ml, respectively. The chemical reaction of lactic acid fermentation is shown below. (5 pts.) C6H12O6 2 C3H6O313. A stock solution of alcohol dehydrogenase (ADH) has been diluted 1 in 10 and the absorbance reading at 280 nm of this diluted solution is 0.04. Given that the absorption coefficient for ADH at 280 nm is e mg/ml = 1.6 and that you require to do 30 assays in triplicate, each assay using 2 ug of enzyme, how many ul of the stock ADH do you need to do the experiment?
- 2. If the KM of an enzyme is 100 µM and it's Vmax = 7.5 µM.s². Calculate %3D initial velocity of the reaction catalyzed by this enzyme when the substrate concentration is 4 mM.1. The initial rate of an enzymatic reaction was determined at different substrate concentrations. The data is below: [S] (μmoles/L) v [(μmol/L) min -¹] 20 50 100 200 65 102 120 135 A. Graph Michaelis and Menten and use it to estimate Vmax and Km. B. Make the Lineweaver-Burk plot and use it to estimate Vmax and Km. C. What would you expect to find in the values of Vmax and Km if you do the same experiment but with twice the amount of enzyme used here. Draw your answer on the MM graph. 2. The Table below shows the data collected by an undergraduate student of the enzyme rate at different substrate concentrations. In the presence and in the absence of an inhibitor.3.An enzyme catalyzed reaction is studied and the following kinetic analysis is obtained: |[S), mM 0.050 0.075 v, (µM min") 0.93 1.264 1.77 2.14 3.7 0.125 0.175 0.935 a. Using Excel, make a fully labeled Lineweaver-Burk plot and determine the Km and Vmax for the enzyme b. The reactions were set up dissolving 1 mg of the enzyme (MW= 100000 Da) in 100 ml of final reaction buffer. Determine the turnover number for the enzyme assuming 1 active site exists per enzyme molecule? c. Determine the catalytic efficiency for the enzyme d. The same reactions are performed in presence of an inhibitor A and the resulting velocities determined: v plus inhibitor, (µM min) 0.272 0.37 0.518 0.626 |1.08 |[S), mM 0.050 0.075 0.125 0.175 0.935 Plot these data on the same graph as above and determine the new Km and Vmax and the type of inhibitor (competitive, non-competitive). e. Can the effects of the inhibitor be over-ridden by adding more substrate? Why?