ncentration of 3 X 10 M. Find the time required to convert 70% of substrate when Vmax = 2.167 M/min. PBL 1: An enzyme with a Km = 1 X 10² M was assayed to convert the substrate with initial co Km So In (So-S) Vmax t = Vmax S = So - xSo
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- 7. 116.5 ug of trypsin (MW 23.3 kDa) was mixed in a 1 ml solution with an excess of a peptide substrate. The reaction is stopped after 10 seconds and the amount of cut peptide is measured to be 3.35 umole. The reaction is repeated with [S] - 0.012 M, and the amount of cut peptide is measured to be 1.175 umole in 10 seconds. a) What is the concentration of enzyme present? b) What is Vm ? c) What is KM ? d) What is kcat ?We have three inhibitor and same enzyme were incubated with 5 mM of substrate and 2 mM of inhibitor.I1,competitive inhibitor, I2,uncompetitive inhibitor, I3, non-competitive inhibitor.Assuming that Vmax = 80 mM s-1 , Km = 8 mM, and KI of all three inhibitors was 10 mM, which of the inhibitors was the most efficient on V0? Explain your answer1. An enzyme-catalyzed reaction has a KM of 1 mM and a Vmax of 5 nM s-1. What is the reaction velocity when the substrate concentration is 0.25 mM? 2. If an enzyme-catalyzed reaction has a velocity of 2 mm/min and a Vmax of 10 mm/min when the substrate concentration is 0.5 mM, what is the KM?
- Calculate the value of the denaturation constant kd for a given enzyme, using the equation provided from the text and lecture of kd = Ad e(-Ed/RT) where Ad = 6.1 x 1047 and Ed = 69 kcal/g mole. Then, prepare a plot of per cent enzyme maximal activity vs temperature using an Ea of 23 kcal/gmole, and an enzyme concentration E0 of unity. Note that the y-axis of this plot is a per cent value, so the value of A in the Arrhenius equation does not need to be known in this case. On the denaturation side of the curve, use 5 minutes as the constant exposure time. Use a temperature range of 20 to 50⁰C.Enzyme X can act on either substrate A or B; the Km on A < Km on B. Vmax for A > Vmax on B.Sketch 1 plot for 1/v vs. 1/[S] plot for Enzyme X in the presence of A and in the presence of B.Plots A and B show enzyme kinetics data in the absence and presence of inhibitor. Which response describes the effect of the inhibitor? Vo (M¹) 10 9 A [S] (mm) 6 8 10 Apparent Km > Km; Apparent Vmax > Vmax Apparent Km > Km; Apparent Vmax Vmax B -1 1.2 1 0.8 0.6 0.4 0.2 0 -0.2 1 1/[S] (mM¹) Analyse the plot and calculate the values. This question is harder than it seems. 2
- Question 15 Plots A and B show enzyme kinetics data in the absence and presence of inhibitor. Which response describes the effect of the inhibitor? B Vo (M¹) 2960 10 A [S] (mm) 6 8 10 Apparent Km > Km; Apparent Vmax > Vmax Apparent Km > Km; Apparent Vmax Vmax -1 1.2 1 0.8 0.6 0.4 0.2 0 -0.2 1 1/[S] (mM¹¹) Analyse the plot and calculate the values. This question is harder than it seems. 2From a kinetics experiment, the Vmax was determined to be 325µM*min^-1. for the kinetic assay, 0.1mL of a 0.25mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 75,000 g/mole. Assume a reaction volume of 700µL. Calculate the kcat (in sec^-1) for the enzymeGiven Epsom salt - https://fscimage.fishersci.com/msds/13510.htm Describe the adverse effects of the substance to newborns or child development during pregnancy. Mutagenic Slightly mutagenic Teratogenic Non-teratogenic Non-mutagenic
- Given the following data for an enzyme-catalyzed reaction. Substrate conc., mM Velocity, mM/s 0.10 0.96 o.125 1.12 0.167 1.35 0.250 1.66 0.50 2.22 1.00 2.63 1.Write the equation of the line consistent with the Lineweaver- Burke equation (type answer in this format: y=mx+b) 2. Calculate the Vmax. 3. Calculate the Km. Please help me. Kindly explain step by step the solution to this problem. Thank you.An enzyme has a Km of 8 M in the absence of an inhibitor and an apparent Km of 12 M in the presence of 3 M of an inhibitor. The Vmax is unaffected by the inhibitor. A. What type of inhibitor is this? B. Calculate KI for this inhibitor.kcat (sec). 500 A 300 100 80 60 R-Ć- The following kinetic data were obtained for this enzyme: 40 4 H 5 6 COO OH pka: 5.1 and 9.6 7 pH kcat/Km (mM¹ sec) 1000 100 8 9 10 4 B 5 pka: 5.5 and 8.9 6 7 PH R- 8 9 10 KIE (VND) 7 6 5 4 3 نا 2 OH H C 4 5 COO pka 6 - 9.4 7 8 PH 9 10 (i) Draw a scheme showing all the protonation states of E (depicted as E, ES, ESH, EH, EH2, etc.) and their equilibria, together with the actual conversion of S (substrate) into P (product), assuming a single intermediate (you do not have to put in the rate or equilibrium constants). (ii) Match up the 4 pKas in the figures, A and B, with the different protonation states. (Explain what the pKas in Figures A and B represent). (iii) The data in Figure C refers to the kinetic isotope effect on the keat, obtained when the H indicated in red in the reaction given above, is replaced with a deuterium. Why does Figure C show only one pka? Given the information in C, together with that of A and B, what can you conclude about…