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 V) versus [S] (concentration) for the carbonic anhydrase reaction. The graph also shows the curve in the presence of acetazolamide. 100 No inhibitor Acetazolamide 0.2 0.4 0.6 0.8 (8) (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. AJO %)A
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- 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 Vmax) 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. (*"A JO %) AFigure I shows the Michaelis Menten plot of initial reaction velocity (as percentage of Vmax) versus [S] (concentration) for the carbonic anhydrase reaction in the absence and presence of the inhibitor acetazolamide. Carbonic anhydrase participates in regulation of the pH and bicarbonate content of a number of body fluids. 100 No inhibitor Acetazolamide 0.2 0.4 0.6 0.8 1 [S] (mM) Figure 1 (i) Compare Vmax and Km of the enzyme without inhibitor and in the presence of acetazolamide. Determine the type of inhibition shown by acetazolamide. Explain your answer. (ii) Name TWO (2) other types of inhibitions besides the inhibition shown by acetazolamide in Qla)(i). List down the kinetic properties of these inhibitions. Sketch a graph of I/V versus 1/[S] showing plots in the absence of an inhibitor and in the presence of the types of inhibitors mentioned in Qla)(ii). (iii) V (% of VmaxWhich of these heterocyclic drugs is likely to be the least soluble in water? Use the Fsp³ parameter to decide. OH Tramadol Chemical Formula: C16H25NO2 YOUR OW Pantoprazole Torasemide Chemical Formula: C16H15F2N3O4S Chemical Formula: C16H20N4O3S Temazepam -OH Chemical Formula: C16H13CIN₂O2 Tioconazole Chemical Formula: C16H13C3N₂OS A. Tramadol B. Pantoprazole C. Torasemide D. Temazepam E. Toconazole
- Determine the Ki for the inhibitor at 30 °Cand decide what type of inhibitor is being used. Eo T I S V (g/I) (°C) (mmol/ml) (mmol/ml) (mmol/ml-min) 1.6 30 0.1 2.63 1.6 30 0.033 1.92 1.6 30 0.02 1.47 1.6 30 0.01 0.96 1.6 30 0.005 0.56 1.6 49.6 0.1 5.13 1.6 49.6 0.033 3.70 1.6 49.6 0.01 1.89 1.6 49.6 0.0067 1.43 1.6 49.6 0.005 1.11 0.92 30 0.1 1.64 0.92 30 0.02 0.90 0.92 30 0.01 0.58 0.92 30 0.6 0.1 1.33 0.92 30 0.6 0.033 0.80 0.92 30 0.6 0.02 0.57From your Lineweaver-Burk plot,the vlaues are: Km Vmax Uninhibited 0.09 mmol/L 3.02 min/mmol Inhibited 6.22 mmol/L 9.98 min/mmol By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.what possible outcome may be produced when the molecular weight of an alcohol antiseptic is increase to a C20, will it still be effective? Explain your answer
- One treatment for hyperuricemia is administration of xanthine oxidase inhibitors like allopurinol. Discuss the mechanism and show an illustration how this drug able to alleviate symptoms of hyperuricemia.Briefly describe the effects of a linear noncompetitive inhibitors on the kinetic parameters Km and Vmax. breifly discuss the reasons behind the effect of this type of inhibition on the kinetic parametersMatch each inhibitor with its effect on Michaelis-Menten reactions. Group of answer choices Vmax and apparent Vmax are equal and the apparent Km is greater than Km. The apparent Vmax is less than Vmax and the apparent Km and Km are equal The apparent Vmax and the apparent Km are both lowered to the same degree. The apparent Vmax is less than Vmax and the apparent Km can be either greater than or less than Km.
- -1/aka 1/v. Increasing a=1 (no inhibitor) Slope = a KµV…... Slope ak 7-15 satino inhibitori B D MELIN H W MIN 061 d'Nat 1/V a = 2 a=1.5 Increasing (1) o1 (no inhibitor) Slope = KNALLENational Board of Medical Examiners Biochemistry Mark 36. In the presence of a metabolite (X), 6-phosphofructokinase is assayed at a fixed concentration of ATP and varying concentrations of fructose 6-phosphate. The resulting data are shown in the table. Fructose 6-phosphate (pM) 5 10 20 40 75 100 200 Velocity umoles/min 0.05 0.15 0.25 0.70 1.7 2.2 3.1 3.1 Velocity (+X) umoles/min 0.006 0.025 0. 10 0.35 1.03 16 2.9 3.1 400 Metabolite (X) is most likely which of the following substances? O A) ADP O B) AMP OC) CAMP D) Citric acid O E) Fructose-2,6-bisphosphate(b) You are investigating the effects of several agents on the activity of alcohol dehydrogenase. The enzyme activity data are shown in the table below. Construct a [substrate] vs. activity plot and a double-reciprocal plot for this enzyme. Be sure to label all axes. Determine the Vmax and KM for AD from the graphs in each type of plot. AD activity (nM/min) AD activity + agent A (nM/min) AD activity + agent B (nM/min) [Alcohol] (nM) 0.1 14 2 0.5 50 7 8. 1.0 65 10 30 2.0 72 12 45 4.0 80 14 62 8.0 85 15 75 32.0 90 16 90