111 The Michaelis constant is represented by what variable, and is comprised of which rate constants in the overa enzyme rate equation? e. Km, kf, k, and k_cat f. Vmax, kf and kcat g. Km, kf, k, and kcat h. Vmax, kf, kr, and kcat i. Km, kf and kcat
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- Refer to the following graph when answering questions. These words may be used to fill: competitive, uncompetitive, noncompetitive, irreversible. -1 mg , μmol min-1 v-1 0.2 0.1 THA -4-2 CBA + 2 4 [S]-1, (mM-1) Word 1, The value of Km for the enzyme depicted by curve A is 2, The value of Vmax for the enzyme depicted by curve A is 3, Curve B depicts the effect of an inhibitor on the system described by curve A. This inhibitor is a inhibitor. 4, Curve C depicts the effect of a different inhibitor of the system described by curve A. This second inhibitor is a inhibitor. DThe growth of a bacterium follows the Monod model with μmax=0.3 h-1, Ks=2.5 g/l and Yx/s=0.20gx/gs. Calculate the number of continuous mixing tank type bioreactors in series, with 10 L of useful capacity each, necessary for the limiting substrate conversion to be greater than 98%, considering that the system is fed with a flow rate of 2.5 L/ h and the substrate concentration in the feed is 30 g/L.roblem 1An aerobic biochemical process uses a CSTR w/o recycle. The feed characteristics are asfollows: Influent substrate concentration, So = 200 mg/L; half- velocity coefficient, Ks = 50mg/L; maximum, specific substrate utilization rate, k = 5 g/g- day; yield coefficient, Y = 0.5g Xa/g substrate consumed; microorganism decay coefficient, b = 0.10 day-1.1. The process goal is the production of active biomass. Determine the hydraulicretention time that the reactor should be operated in order to maximize the reactoractive biomass concentration (Xa). How does this retention time compare with theminimum solids retention time that the system can theoretically be operated?Calculate the solids retention time safety factor.2. Based on the solids retention time for maximum Xa calculated above, estimate theactive biomass concentration (Xa) and the substrate removal efficiency (E, %)
- Consider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?You were asked to determine the mode of inhibition exerted by Inhibitor DEDS to a newly discovered enzyme known as BILISTASE. The kinetics data are shown below: [Substrate, µM] Vo with DEDS (µM/min) Vo without DEDS (uM/min) 1.667 1.600 3.544 12.500 1.923 4.259 13.333 2.139 4.737 %3D 14.000 2.268 5.019 5.000 2.410 5.336 Using linear regression analysis, determine the values of Vmax and KM of the enzyme in the ABSENCE of inhibitor: (Express your answer in 3 decimal places, do NOT include the units) Vmax = KM=i) Re-arrange the Michaelis Menten equation so it involves the ratio [S]. Show all steps beginning Km noting any assumptions or required conditions. Km ii) Calculate the ratio [lo for the case when the rate of product formation is 68% of Vmax and the substrate is in great excess. d[P] dt : k₂ with = [E],[S] Km+[S]' [S]o Km iii) Explain, in a few sentences, why the ratio determines the ratio V Vmax V Vmax Begin by explaining the meaning of stating simply "it's the ratio...." is not sufficient. Include in your explanation the factors that effect v and Vmax. Consider what factors make v different from or equal to Vmax. Consider what Km represents concerning processes involving ES. " iv) Calculate KM at 310K at given the following rate constant information: k₁ = 17 s-¹M-1 at 300K with A = 7300 s-¹M-1 K-1₁ 6 s¹ at 300K with A = 14500 s -1 k₂ = 31 s¹ at 300K with A = 600 s-¹
- The equil ibrium constant for the attachment of a substrate to the active site of an enzyme was measured as 200.In a separate experiment, the rate constant for the secondorder attachment was found to be 1.5 x 108 dm3 mol-1 s- 1.What is the rate constant for the loss of the unreacted substrate from the active site?A scientist is studying the enzyme X which is an important point of regulation in the metabolism of the inhabitants of Sumeru. He developed four Akademiyan-derived compounds which may possibly work against this enzyme, and tested using an eudiometer the metabolic rate of the sample cell lines. Data are below. Time for each compound (min) Eudiometer volume reading (mL) A B C D 0 83.1 62.6 89.0 66.4 5 83.2 100.6 90.2 71.4 10 83.2 83.6 95.0 77.2 15 83.2 83.6 100 84.6 20 83.3 110.8 104.6 88.2 Show the properly labeled volume versus time plot for each eudiometer, with the equation of the line and R2. What is the most effective inhibitor among the four compounds? It was found that the most effective inhibitor exhibits uncompetitive inhibition. Illustrate the Lineweaver-Burk plots of uninhibited and inhibited enzyme X with properly labeled axes.Calculate the Vmax of the above enzyme (lactase). (the enzyme lactase has a Vo of 0.111111111111 mM per minute when [S] = 1.0 mM, and a Vo of 0.20 mM per minute when [S] = 5.0 mM) 0.125 mM per minute 0.25 mM per minute 0.50 mM per minute 1.25 mM per minute 5.0 mM per minute
- Consider the Michaelis-Menten equation, below: Vmaz (S V. k + [S] %3D What is the relationship between changes in substrate concentration and velocity when the concentration of substrate, [S), is well below k7 The S terms cancel out in this equation, so there is no effect of changing substrate concentration. The S] term in the numerator is negligible, so there is no impact of changing substrate concentration. Because the enzyme has reached Vr there is no effect of changing substrate concentrations on enzyme velocity. OThe [S term in the denominator is negligible compared to k There is a linear relationship between substrate concentration and velocity.Part a) Which graph has the largest kcat? Please explain. Part b) Which graph has the tightest substrate binding? Please explain. Part c) Which graph has the largest specificity or efficiency constant? Please explain.Example 14.6 The oxygen requirement for cell growth in glueose can be represented by the following equation (Mateles, 1971) 32NC+8(Nh2)+16(No2) Fx/sM +yo2 – 2.67yc + 1.714YN2 – 8y H2 ro2 = In which ro2 is the oxygen required for each gram of cells produced, N stands for no. of atoms present in each molecule substrate, y stands for mass fractions and M is the MW of the substrate. The yeast cell may be considered to be CH1.800.5NO.2. Calculate rO2 if the yield factor (Yx/s) is 0.46g of cells produced for each gram of substrate consumed.