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- Two different preparations of the same enzyme are characterized below. Total protein (mg) Total activity (activity units) Step Volume Specific activity (ml) Preparation 1 300 1000 600,000 Preparation 2 200 1000 500,000 a) Fill in the 3 double-underlined blanks on the table below. b) Which of the 2 preparations would you think is likely to be more pure? Explain.You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphatasea) Based on the data shown in the image, what are the Km and Vmax for the enzyme with L-DOPA and D-DOPA? Show any relevant analyses or calculatins you did to determine these values. ( HINT a graph might be helpful here! ) b) Based on your answer to part a, briefly describe how the kinetics of the enzyme differs for the two substrates. Which Substrate has better binding affinity to the enzyme
- Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-1. Outline and describe the reaction scheme of the production of glucose from maltodextrin by using glucoamylase.The protein catalase catalyzes the reaction 2H,O,(aq) — 2H,O(l) + O,(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s¯¹. The total enzyme concentration is 0.010 µM and the initial substrate concentration is 4.83 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax Calculate the initial rate, R (often written as V), of this reaction. R = ×10 mM.s-1 mM-s-1The lipase substrate emulsion contains 0.500 mg of olive oil per 3 mL Also, the molar mass of the olive oil is 885 g/mol. If all of the olive oil in a 3 mL reaction is "digested" by pancreatic lipase in a reaction, how many molecules of olive oil have been degraded?
- when saturated with substrate, an enzyme has a maximum initial rate of 110mumoles of substrate converted to product per second. At a substrate concentration of 100mu M, the same enzyme converts substrate to product at a rate of 0.010mmoles/ sec. Assuming that Michaelis - Menten kinetics are followed, calculate the reaction rate when substrate concentration is 2x10^-3M.After purifying alkaline phosphatase, you perform enzyme kinetic experiments with and without an inhibitor to obtain the following plot: With inhibitor Without inhibitor 1/V (1/mM min?) 0.3 0.2 -150 -100 -50 50 100 150 200 250 300 1/s (1/mM) a) What is the name given to this type of enzymatic plot? b) Using the graph, calculate K_ and V_ inhibitor. Show all calculations. for the enzyme, with and without the maxA solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates. It is impossible for this result to be true. OA. Adding the substrate increases the weak forces that stabilize the enzyme. OB. The high concentration of substrate forms a barrier around the hexokinase. D. Adding the substrate results in protective covalent bonding.
- Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.The process of protein decomposition by pepsin enzymes in stomach is assumed and modeled as a batch reactor. If the protein concentration over time is measured as follows: Write the relationship between time (t), protein concentration (CA). Assuming that the enzyme reaction follows Michaelis-Menten kinetics, write the required constant (Vmax, Km), and the initial concentration of the protein is CA0.The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"
