parameters of AP. İndicate the value for the activity of AP(which is 3.08) What does it mean? Is your enzyme active or not? What does it say about the purity of your enzyme? How the purification process affects the activity?
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- a) Determine kcat (in units of sec-1) for a particular enzyme, given the following information: Vo = 144 mmol/min; [S] = 2 mM; Km = 0.5 mM; Enzyme Molecular weight = 40,000 mg/mmole; 8 mg of enzyme used in assay generating this data. b) In general, explain how the total enzyme concentration affects turnover number and Vmax?The turnover number for an enzyme that approximates Michaelis-Menten kinetics is known to be 500 min^-1. From the results shown in the table, enumerate Km and total amount of enzyme present. What is the Km for this enzyme? What is the Vmax for this enzyme? And what is the [E]T for this enzyme?Assume that the experiments performed in the absence of inhibitors were conducted by adding 5 μL of a 2 mg/mL enzyme stock solution to an assay mixture with a total volume of 1 mL. Take into account that XYZase is a monomeric enzyme with a molecular mass of 45,000 Daltons. Hint: To calculate the ???? in units of per second (s−1), you must first determine the ???? in micromoles per second (μmol/sec). Please explain step by step
- The Keq (25C) of the reaction below is 635.67. Fructose 1,6-biphosphate <-->fructose -6-phosphate + Pi. a) What is the standard Gibbs free energy change for this reaction? b) if the concentrationof fructose 1,6 biphosphate is adjusted to 0.85 M and that of fructose 6 phosphate and phosphate adjusted to 0.055 M, what is the actual free energy changeWhile furthering your studies of iocane powder you determine that a ceular enzyme, iocase will degrade it. Under normal conditions, iocase shows km 0f 1.85 uM and a kcat of 76. The drug sildenafil was found to have no effect on the km of iocanse yet the kcat was found to drop 58 minutes^-1, when the drug was added and no other changes were made in the reaction conditions. What can be inferred from this data? (remember kcat = vmax/et) Sildenafil acts as an uncompetitive inhibitor of iocanse Sildenafil acts as a noncompetitive inhibitor of iocanse The effect of sildenafil could be countered by adding more iocane to the reaction The y-intercept of the sildenafil inhibited iocanse would appear to be lower on a Lineweaver burke plot as compared to uninhibited iocanase The slope of a Lineweaver burke plot of the inhibited versus uninhibited iocanase would remain unchangeda. Estimate KM and Vmax for the uninhibited reaction from the first graph. Whatdifficulties do you find in getting accurate values?b. Make a Lineweaver-Burk (double reciprocal) plot to determine KM and Vmax again.What advantages do you see with the second method? c. Use the Lineweaver-Burk method and the table of data for the inhibitors to determine the kind of inhibition for each inhibitor.
- Give an example of a noncompetitive inhibitor and its target enzyme. Draw a hypothetical Michaelis-Menten curves in the presence and absence of the noncompetitive inhibitor. Discuss the effects of noncompetitive inhibition and the reasons for these effects on the values of Km and Vmax.Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions: (a) How do I run the experiment to find the kinetic properties of the enzyme, KMand Vmax? (b) The enzyme decreased in activity in the presence of NaCl. How do I find out if NaCl is a competitive or non-competitive inhibitor? Explain.Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.
- What is the rate of the reaction at 20 sec for each of the enzyme concentration. Show calculationMost of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: Give the Michaelis-Menten equation of an enzyme reaction and draw the Michaelis-Menten plot of [S] versus V0.A TAMU undergraduate biochemistry student is tasked with characterizing a new enzyme. After devising an assay, the student does some initial experiments. When initiating the reaction by adding the enzyme to a solution of substrates (but no products) she finds that at the earliest times the change in the [A] is non-linear and increasing and then becomes linear for awhile and then decreases eventually to zero. Explain what is unusual and what various aspects of the time course mostly likely means.