2.1. For an enzyme (5µM), the following initial velocities have been reported depending on the substrate concentration: [Substrate], mM Vo 0.02 10.83 0.04 18.57 0.07 26.76 0.1 32.50 0.15 39.00 0.2 43.33 0.3 48.75 0.5 54.17 0.7 56.88 2.2. Sketch the Eadie-Hofstee plot for the enzyme reaction 2.3. Determine Km and Vmax for this enzyme 2.4. Indicate where Vmax and Km can be recognized
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- For an enzyme that follows Michaelis –Menten kinetics, k1=1X106 M-1 sec-1, k-1= 2x103 sec-1 and k2=2X 102 sec-1. a. What is the Km for the enzyme ? If the enzyme concentration is 10 nanomoles in 1 ml, what is Vmax for the enzyme ? What is the catalytic efficiency for this enzyme?A research group discovers a new version of happyase, which they call happyase*, that catalyzes the chemical reaction The researchers begin to characterize the enzyme. a)In the first experiment, with [Et] at 4 nM, they find that the Vmax is 1.6 μM s-1. Based on this experiment, what is the kcat for happyase*? (Include appropriate units.) b)In another experiment, with [Et] at 1 nM and [HAPPY] at 30 μM, the researchers find that V0300 nM s-1. What is the measured Km of happyase* for its substrate HAPPY? (Include appropriate units.) c)Further research shows that the purified happyase* used in the first two experiments wasactually contaminated with a reversible inhibitor called ANGER. When ANGER is carefully removed from the happyase* preparation, and the two experiments repeated, the measured Vmax in (a) is increased to 4.8 μM s-1, and the measured Km in (b) is now 15 μM. For the inhibitor ANGER, calculate the values of αand α’.(a) Most commercial heterogeneous catalysts are extremelyfinely divided solid materials. Why is particle sizeimportant? (b) What role does adsorption play in the actionof a heterogeneous catalyst?
- An enzyme-catalyzed reaction is studied in the absence and presence of an inhibitor and the following data was obtained. [S] in mmoles/L Velocity in mmoles/L/min-1 No inhibitor With inhibitor 1.25 1.72 0.98 1.67 2.04 1.17 2.50 2.63 1.47 5.00 3.33 1.96 10.00 4.17 2.38 Calculate the Km of the enzyme in the reaction without inhibitor ________________________ Km’ of the enzyme in the reaction with inhibitor ________________________ Vmax of the uninhibited reaction ________________________ Vmax’ of the inhibited reaction ________________________An enzyme-catalyzed reaction has a Km of 1.4 mM and a Vmax of 7 nM/s. What is the initial velocity when the substrate concentration is 0.6 mM?6. What is the instantaneous reaction rate for an enzyme system? k = 0.087 1/h; enzyme concentration = 0.02 M; substrate concentration = 0.05 M; and Km concentration = 0.01 M? Answer should be in units of mM/h
- Determine the average rate of change of BB from ?=0 st=0 s to ?=272 s.t=272 s. A⟶2BA⟶2B Time (s) Concentration of A (M) 0 0.7300.730 136136 0.4450.445 272272 0.1600.160 rateB= __________M/sThe enzyme-catalysed conversion of a substrate at 25 oC has a Michaelis constant of 0.015 mol dm-3 . and a max-imum velocity of 4.25 x 10-4 mol dm-3 s-1 when the enzymeconcentration is 3.60 x 10-9 mol dm-3. Calculate koat and the catalytic efficiency η. Is the enzyme 'catalytica lly perfect'?An enzyme kinetics experiment is carried out by adding 1.00mg of a 50.0kDa enzyme into a total volume of 50uL of buffer, and measuring the initial rates while adding increasing amounts of substrate (1 Da = 1 g/mol). The calculated Vmax from this series of experiments was 30.5mM/s. Calculate the turnover number for the enzyme.
- A An enzyme that follows Michaelis-Menten kinetics has a KM value of 16.0 uM and a kcat value of 181 s-1. At an initial enzyme concentration of 0.0100 uM, the initial reaction velocity was found to be 1.07 x 10- uM/s. What was the initial concentration of the substrate, [S], used in the reaction ? Express your answer in micromolar to three significant figures2AB2(g) = A2(g) + 2B2(g) A 500,0 ml ask is filled with 0,384 mol of AB2. the appearance of A2 is monitored at timed intervals. assume that temprature and volume are kept constant. the data obtained are shown in the table below. time/min : 0 10 20 30 40 50 moles of A2 : 0 0,0541 0,0833 0,1221 0,1432 0,1567 a. make a similiar table for the dissapearance of AB2 b. what is the average rate of dissapearance of AB2 over the second and the third 10 minutes intervals? c. what is the average rate of appearance of A2 between t=30 and t=50?For an enzyme that displays Michaelis-Menton kinetics, what is the reaction velocity, V (as a percentage of Vmax, observed at the following values? [S] = KM [S] = 0.5KM [S] = 0.1KM [S] = 2KM [S] = 10KM