Calculate vi and the degree of inhibition caused by a competitive inhibitor under the following conditions: (a) [S]=2x10-3 Mand[I]=2x10-3 M (b) [S]=4x10-4 Mand[I]=2x10-3 M (c) [S]=7.5x10-3 Mand[I]=10-5 M Assume that Km = 2 x 10-3 M, Ki = 1.5 x 10-4 M and Vmax = 270 nmoles x liter-1 x min-1.
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Problems 14 and 15: some of the exponents are unclear. Here they are:
14. Calculate vi and the degree of inhibition caused by a competitive inhibitor under the following conditions:
(a) [S]=2x10-3 Mand[I]=2x10-3 M
(b) [S]=4x10-4 Mand[I]=2x10-3 M
(c) [S]=7.5x10-3 Mand[I]=10-5 M
Assume that Km = 2 x 10-3 M, Ki = 1.5 x 10-4 M
and Vmax = 270 nmoles x liter-1 x min-1.
The degree of inhibition is the percent of the uninhibited velocity reached in the presence of the inhibitor.
15. (a) What concentration of competitive inhibitor is required to yield 75% inhibition at a substrate concentration of 1.5 x 10-3 M if Km =2.9x10-4 M and Ki =2x10-5 M? (b)Towhatconcentration must the substrate be increased to reestablish the velocity at theoriginal uninhibited value?
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- 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)…
- (1) Enzy Matic, a Biochemistry student is studying the mode of inhibition of maleate to fumarase enzyme. Fumarase is the enzyme in the Kreb's cycle that converts fumarate to malate. He obtained the following kinetics data from her experiment: Velocity (mM/min) Inhibited 1.38 [S], mM Uninhibited 1.75 1.94 2.17 3.00 5.50 2.26 1.67 2.85 3.55 2.13 2.97 10.5 4.39 3.83columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 Им. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and Ky for the enzyme a. C. e. [S] (mM) (1) V. {(umol/(ml.s)] (2) V. [[umol/(ml.s)]| 4.4 (3) V. umol/{ml.s] 6.6 11.4 76 14.6 8.6 26.6 16.4 29 8 17.8 24.6 28.2 16 45.8 24 60 40.8PROBLEMS 8.1 An enzyme-catalysed reaction was found to be affected by two inhibitors A and B. The following results were obtained at fixed total enzyme čoncentration: Substrate conc" Initial velocity (absorbance units per minute) (mmol l-) With 1 mmol I-B Uninhibited With 1 mmol l- A 0.684 50 20 1.08 0.653 0.468 10 1.43 1.01 0.649 0.476 0.374 0.311 5 1.02 0.363 0.798 0.657 3.3 0.296 2.5 0.250 2.0 0.549 Comment on these results. 8.2 The system investigated in problem 7.1 was investigated again under identical conditions but in the presence of an inhibitor, giving the following data: 40.0 6.67 10.0 156 20.0 Substrate conc" (mmol 1-1) Initial velocity (umol 1- min-1) 5.0 100 122 222 278 Determine the type of inhibition. If K, for this system is 2.9 mmol 1-', calculate the inhibitor concenträtion present.
- PROBLEMS 8.1 An enzyme-catalysed reaction was found to be affected by two inhibitors A and B. The following results were obtained at fixed total enzyme čoncentration: Substrate conc" Initial velocity (absorbance units per minute) (mmol l-) With 1 mmol I-IB Uninhibited With 1 mmol I-1À 50 20 0.684 1.08 0.653 1.01 0.649 0.476 0.374 0.311 10 1.43 0.468 1.02 0.363 0.296 3.3 0.798 2.5 2.0 0.657 0.549 0.250 Comment on these results.Question: A. To explore the consequences of coupling ATP hydrolysis under physiological conditions to a thermodynamically unfavorable biochemical reaction, consider the hypothetical transformation X⟶Y, for which Δ?′°=20.0 kJ/mol. What is the ratio of [Y]/[X][Y]/[X] at equilibrium? B. Suppose XX and YY participate in a sequence of reactions during which ATP is hydrolyzed to ADP and Pi. The overall reaction is X+ATP+H2O⟶Y+ADP+Pi Calculate [Y]/[X] for this reaction at equilibrium. Assume that the temperature is 25.0 °C and the equilibrium concentrations of ATP, ADP, and Pi are 1.00 M each. C. We know that [ATP], [ADP], and [Pi] are not 1.00 M under physiological conditions. Calculate [Y]/[X] for the ATP‑coupled reaction when the values of [ATP], [ADP], and [Pi] are those found in rat myocytes. Metabolite Concentration in rat myocytes (M) ATP 8.05x10-3 ADP 0.93x10-3 Pi 8.05x10-3MATHEMATICAL For an enzyme that displays MichaelisMenten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? (a) [S]=KM (b) [S]=0.5KM (c) [S]=0.1KM (d) [S]=2KM (e) [S]=10KM