Calculate the specific activity and kcat for this enzyme
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- The turnover number for an enzyme is known to be 5000min-1. Given the following set of data, Substrate concentration(mM) 1, 2, 4, 6, 100, 1,000 Initial Rate(micromol/min) 167, 250, 334, 376, 498, 499 a) What is the Km of the enzyme for the substrate? (do this without using a calculator) b) What is the total amount of enzyme present in the assay?Briefly comment on the differences of using a fixed-time assay versus a kinetic assay to measure enzyme activity. Is it reasonable to assume that the reaction velocity obtained by measuring the amount of product after 30 minutes in a fixed-time assay is directly proportional to absorbance? How could you determine whether this was the case? Word limit 180 words including citation and reference200 ml of a 2% protein solution are available, containing an enzyme to be purified. Half of the sample is subjected to method A, consisting of fractionated precipitations, and 5 ml of final solution are obtained, with a protein concentration equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml is obtained, with a protein richness equal to 10 mg / ml, and with an enzymatic activity equal to 2000 U / ml. You want to know: a) Which of the methods has provided the purest enzyme. b) By which of the methods has the greatest amount of protein been obtained.
- The initial velocity data shown in the table were obtained for an enzyme. Each assay at the indicated substrate concentration was initiated by adding enzyme to a final concentration of 0.01 nM. Derive Km, Vmax, kcat, and the specificity constant. [S] (mM) Velocity (x10^7) 0.10 0.96 0.125 1.12 0.167 1.35 0.250 1.66 0.50 2.22 1.0 2.63If the data from an enzyme experiment is plotted as a Lineweaver-Burk plot, and the Vmax is 0.02 mol/sec, and x-intercept is –2.5 mM then what is the KM value? Show yourwork/reasoning.From a kinetics experiment, Kcat was determined to be 55sec^-1. For the kinetic assay, 0.05mL of a 0.05mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 30,000g/mole. Assume a reaction volume of 3mL. Calculate Vmax (um*min^-1) for the enzyme and catalytic efficiency (in M^-1sec^-1) for the enzyme. The Km for the enzyme was determined to be 8.3*10^-2M.
- DNS reaction is an alternative assay for enzyme activity .What is involved or basis for this reaction?From a kinetics experiment, kcat was determined to be 295sec-1. For the kinetic assay, 0.3mL of a 0.25mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 3mL. Calculate Vmax (µM∙min-1) for the enzyme and catalytic efficiency ( in M-1sec-1) for the enzyme. The Km for the enzyme was determined to be 2.55 x 10-2M.200 ml of a 2% protein solution containing an enzyme that you want to purify. Half of the sample is subjected to method A, consisting of fractionated precipitations and 5 ml of final solution are obtained, with a concentration protein equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml, with protein richness equal to 10 mg / ml and with an activity enzymatic also equal to 2000 U / ml. You want to know: a) Which of the two methods has provided the purest enzyme. b) By which of the methods the greatest amount of enzyme has been obtained.
- A biochemist discovers and purifies a new enzyme, generating the purification table below. Procedure Total Protein (Mg) Activity (Units) Crude Extract 20,000 4,000,000 Precipitation (Salt) 5,000 3,000,000 Precipitation (pH) 4,000 1,000,000 Ion Exchange Chromatography 200 800,000 Affinity Chromatography 50 750,000 Size-exclusion Chromatography 45 675,000 a) From the information given in the table, calculate the specific activity of the enzymeafter each purification procedure.b) Which of the purification procedures used for this enzyme is most effective (i.e., givesthe greatest relative…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?Lisa decides to obtain values for the Km and Vmax of an enzyme that was isolated from liver cells.. Using the Michaelis Menten plot. In what kind of measurements are needed and what would be needed to plot on a graph to estimate Km and Vmax?
