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.
Suppose that the following data are obtained for an enzyme-catalyzed reaction: [S] (mM) V (mmol ml-1min-1)...
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
Consider the data collected for an enzyme-catalyzed reaction [S] (mM) vo (mM s1 0.25 2.00 0.50 3.33 1.00 5.00 2.00 6.67 Determine Vmax and K,,m for this reaction. mM s- Vmax mM
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
4. The following data were obtained from an enzyme kinetics experiment. Graph the data using a Lineweaver-Burk plot and determine, by inspection of the graph, the values for Km and Vmax. ISI (M) V (nmol/min) 0.20 0.26 0.33 1.00 1.43 1.67 2.08 3.33 5. You measured the kinetics of an enzyme activity as a function of substrate concentration (see Table). The enzyme concentration was maintained constant at a level of 1 M. [S] AM Vopmol/min 2.9 3.8 4.4 Plot the...
Consider the data collected for an enzyme-catalyzed reaction. [S] (MM) 2 (MM :5-1) 0.20 0.86 0.33 1.20 2.00 2.42 4.00 2.69 Determine Vmax and Km for this reaction. mMs-1 Km = mM
The following data was obtained for an enzyme in the absence of an inhibitor, and in the presence of two different inhibitors. The concentration of each inhibitor was 10 mM. The total concentration of enzyme was the same for each experiment. [S] {mM} without inhibitor v, {umol/(ml*s)} with inhibitor A v, {umol/(ml*s)} With inhibitor B v, {umol/(ml*s)} 0.0 0.0 0.0 0.0 1.0 3.6 3.2 2.6 2.0 6.3 5.3 4.5 4.0 10.0 7.8 7.1 8.0 14.3 10.1 10.2 12.0 16.7 11.3...
Attempt 2 Question 19 of 41 Consider the data collected for an enzyme-catalyzed reaction. [S] (mM) 0.20 0.37 0.50 0.83 2.22 2.00 3.08 4.00 Determine Vmax and Km for this reaction 9.9999 mM s-1 Vmax 0.9999 Km mM =
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...
Prostaglandins are a class of eicosanoids (fatty acid derivatives) with a variety of extremely potent actions on vertebrate tissues. They are responsible for producing fever and inflammation and its associated pain. Prostaglandins are derived from the 20-carbon fatty acid, arachidonic acid, in a reaction catalyzed by the enzyme, prostaglandin endoperoxide synthase. This uses oxygen to convert arachidonic acid to PGG2 (a prostaglandin). Ibuprofen inhibits this enzyme and is a fever reducer and anti-inflammatory agent. The kinetic data is given below...
s- (3 pts) The flowing rates have been an enzyme- catalyzed reaction at various substrate concentrations: Run no. 103 [S]M Rate, v/ (Ms') 2.41 3.33 4.78 6.17 7.41 9.52 0.0 12.5 0.4 0.6 4 2.0 4.0 a- From Line-Weaver double reciprocal plot, obtain and Mechaelis-Menten constant, max b- If the enzyme concentration is 1.00 x 10-11 M calculate kz.