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 Acetazolamide 0.2 0.4 0.6 0.8 (S) (mm) Figure 2 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. (i) (*"A JO %) 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 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 %) 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 0.57The Mechanism of Action of Cyclophosphamide and its toxicity reference :http://dx.doi.org/10.3390/scipharm88040042 (reseach paper DOI plz answer in detail do not give short answer )From 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.
- 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.National 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-bisphosphateCarbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!
- Match 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 = KNALLEHow was thermal stability measured in this paper and describe how GRL-1720 and 5h affect the thermal stability of Mpro and which drug has the larger effect? https://www.nature.com/articles/s41467-021-20900-6