1. Alpha-glucosidase has a molar mass of about 40 kilodaltons. If 0.50 grams of the enzyme is dissolved in 250 mL of buffer, calculate Kcat for the enzyme with and without quercetin Note: Vmax for the reaction without quercetin = 0.6666 Vmax for the reaction with quercetin= 0.3333
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- 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.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.The catalytic activity of an insect aminopeptidase was investigatedusing an artificial peptide substrate. The Vmax was 4.0 × 10-7 M/s and the KM was 1.4 × 10-4 M. The enzyme concentration used in the assay was 1.0 × 10-7 M. What is the value of kcat? 2.86 x 10-3 M 0.25 M/s 4.0 s-1 2.86 x 104 s/M 0.25 s-1
- An antibody X binds to an antigen Y. When the antigen concentration is 8.0× 10–8 M, θ is 0.90. What is the dissociation constant, Kd, of the antibody for the antigen?An enzyme is needed to be stored in a buffer solution with a pH of 10.00. Unfortunately, only three buffer systems are available in their laboratory: Buffer System Weak Acid Component Ka Conjugate Base Salt PAH Benzoic acid, C6H5COOH 6.25 x 10-5 NaC6H5COO SAD Boric acid, H3BO3 5.81 x 10-7 NaH2BO3 DOH Hydrogen cyanide, HCN 6.20 X 10-10 NaCN In what buffer system (PAH, SAD, or DOH) will Phoebe store the enzyme? (show calculations and briefly explain) Write the equilibrium reaction involved in the buffer system. Calculate the amount (in mL) of the 2.00 M stock solution (pH 10.00) of the same buffer system needed to prepare 250 mL of a 0.650 M buffer pH 10.00.Calculate the specificity constant for an enzyme-catalyzed reaction if the total enzyme concentration is 15 nM, Vmax is 9 M/s, and Km is 150 M. A. Has the enzyme achieved catalytic perfection? (Y or N)
- 3) The enzyme aldolase catalyzes the conversion of fructose-1,6-diphosphate (FDP)to dihydroxyacetone phosphate (DHAP) and glyceraldehide-3-phosphate (G3P). Thereaction isFDP ⇄ DHAP + G3P , ∆rG0(298.15 K) = 23.8 kJ mol−1In red blood cells the concentration of these species are [FDP] = 35 µM, [DHAP] =130 µM, and [G3P] = 15 µM. (Remember that 1.0 µM = 1.0 × 10−6 mol L−1. Thestandard state for reactions in solution can be taken as c0 = 1.0 mol L−1).Calculate ∆rG in a red blood cell at 25 0C. Will the reaction occur spontaneouslyin the cell at this temperature?Carbonic anhydrase is one of the fastest enzymes known. If 10 µg of this enzyme catalyzes the conversion of 0.30 g of CO2 to bicarbonate in 1 minute at 37˚C. What is the Kcat value for this enzyme in min -1?An enzymatic assay was performed using the enzyme phophofructokinase-1, which catalyses the committed step of the glycolysis pathway. What is the final concentration of the fructose 6-phosphate substrate in a test tube containing the following: 250 µL of 150pM fructose 6-phophate, 100 µL 20 mg.ml-1 phosphofructoskinase-1 and 150 µL 100mM buffer pH 7.5
- At a steady state in the living cell, (ATP) = 10-3M and (ADP) = 10-4 M. The maximum(equilibrium) value of the ratio (glycerol-1-P)/(glycerol) is observed to be 770 at 25 Cand pH=7.a. Calculate K and rG for the reaction.b. Using the value of rG for the reaction ADP + Pi →ATP + H2O, together with the answer topart (a), calculate rG and K for the reaction: glycerol + phosphate→ glycerol-1-phosphate+ H2O4 1. Use the Michaelis-Menten equation to explain relationship between the amount of product produced and the concentration of enzyme in each reaction. 2. Briefly explain how you would modify the experiment performed in part C to determine the Km and Vmax of the lactase enzyme ANSWER BOTHA protein has a stability ranging from 6 to 15 kcal/mole at 37 OC. Stability is a measureof the equilibrium between the folded and unfolded protein given by the relationship; folded(F) = unfolded (U), k=[U]/[F] For a protein with a stability of 10 kcal/mole, calculate the fraction of unfolded proteinthat would exist at equilibrium at 37 OC. Use the following equation:GO=RTlnk=-2.3RTlog k,where R=1.98 x 10-3 kcal/mole and T is temperature in Kelvin (K) and k is theequilibrium constant.