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11. Calculate KM and Vmax from the following data: [S] (UM), (mm/s) 0.1 0.34 0.53 0.4...
1. Calculate KM and Vmax from the following data: vo (mM S- 0.34 0.53 0.74 0.91 1.04 [S] (μΜ) 0.1 0.2 0.4 0.8 1.6 1. Calculate KM and Vmax from the following data: vo (mM S- 0.34 0.53 0.74 0.91 1.04 [S] (μΜ) 0.1 0.2 0.4 0.8 1.6
The following data set was collected from an experiment conducted in the lab where a new enzyme is being characterized. Use the Lineweaver-Burk method in order to determine the values of KM and Vmax. Complete your work on a separate piece of paper and upload the excel file or picture of your work. Your work must include the following: Table of reciprocals Reciprocal plot (straight-line graph) Calculations and results for KM and Vmax In order to get full credit for...
Can help me with these questions please. 30. Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below. Sphingosine (uM) vo (mg /min) vo (mg /min) with inhibitor 2.5 32.3 8.5 3.5 40 11.5 5.0 50.8 14.6 10 72...
The value of Km for the shown data for a hexokinase-catalyzed reaction is with the unit of . The value of Vmax for. the same reaction is with the unit of . Be sure to give the values with the correct number of significant figures. You might have to construct a kinetic plot. For units, choose one answer from (uM, 1/ UM, HM/second, uM x second, mM, 1/mM, second, 1/second, mM/second, mM x second) vo (mM/sec) Glucose concentration (mm) 0.10...
3.33 3. Suppose that the following data are obtained for an enzyme-catalyzed reaction: [S(mm) V (mmol ml-Imin-1) 0.1 0.2 5.00 7.14 8.0 1.0 8.33 9.09 (a) From a double-reciprocal plot of the data, determine Km and Vmax. (b) Assuming that the enzyme present in the system had a concentration of 10-6 M, calculate its turnover number 0.8 2.0
Suppose that the following data are obtained for an enzyme-catalyzed reaction: [S] (mM) V (mmol ml-1min-1) 0.1 3.33 0.2 5.00 0.5 7.14 0.8 8.0 1.0 8.33 2.0 9.09 a.) From a double-reciprocal plot of the data, determine Km and Vmax. b.) Assuming that the enzyme present in the system had a concentration of 10-6 M, calculate its turnover number.
Determine the km and vmax from this data. 1/[S] 0.1 0.033333333 0.02 0.01 0.006666667 0.002 1/V0 34.3 31.95 27.2 25.51 20.16 19.6
Here is a question to be sure you are able to calculate Km and Vmax from axes from a Lineweaver-Burk plot. If the y-intercept of a given plot is 0.25 min/uM and the slope is 0.65 min, what are the values of Vmax and Km for this given enzyme? Please Include the work.
An enzyme catalyzes a reaction with a Km of 9.00 mM and a Vmax of 3.95 mM·s–1. Calculate the reaction velocity, v0, for the following substrate concentrations: A. 1 mM B. 9 mM C. 11 mM
Please show how to calculate Km and Vmax for no inhibitor/low inhibitor given graph. Show how to solve for a.,a/a etc. Lineweaver Burk #4: No inhibitor, Low inhibitor 0.2 ▲ No inhibitor Low inhibitor 0.15 0.05 0.2 0.15 0.1 0.05 0.05 0.1 0.15 02 5 1/IS] in units of 1/mM Fill in the blanks. Show your work. No inhibitor Kmno Vmax,o- Vmax,w = ๙ Vmax,o Solve for ๙ inhibitor Krmkw =픕Km,o Solve for 픕 Hint treat, as a single number....