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(15 points) Consider the following reaction: CO2+H20 F HCO; +H* This reaction is catalyzed by the...
Need help with number 13! I already asked about number 12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the...
Need help with number 13! I already asked about number
12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
The following question focuses on how the parameters regulating enzyme function might change, and how these...
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menton plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. see for instance: http://en.wikipedia.org/wiki/Carbonic_anhydrase 1 Assume that one variant has a Km of 1 µM and a different variant has a Km of 10 µM....
Suppose that the following data are obtained for an enzyme-catalyzed reaction: [S] (mM) V (mmol ml-1min-1)...
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.
The following data were recorded for the enzyme-catalyzed reaction. Substrate concentration (M) 6.25 x 100 7.50...
The following data were recorded for the enzyme-catalyzed reaction. Substrate concentration (M) 6.25 x 100 7.50 x 10 1.00 x 10-4 1.00 x 10-3 Reaction velocity (nM/min) 15 56 60 75 (1) Estimate Km and Vmax- (2) What would V be at S=2.5 x 10-5 ?
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
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...
3.33 3. Suppose that the following data are obtained for an enzyme-catalyzed reaction: [S(mm) V (mmol...
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) 2 (MM :5-1) 0.20 0.86 0.33...
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
(15 points) The following data is for a reaction catalyzed by tyrosine monoxygenase: Substrate Concentration (mol/L) ...
(15 points) The following data is for a reaction
catalyzed by tyrosine monoxygenase:
Substrate
Concentration
(mol/L)
Initial Velocity (mM/min)
1.5
0.66
1.2
0.65
0.81
0.45
0.65
0.39
0.49
0.32
0.27
0.21
a) Plot the velocity (y-axis) versus substrate
concentration [S] (x-axis) curve and insert/draw the graph in the
space below. What are the approximate KM and
Vmax values?
b) Construct a 1/v (y-axis) versus 1/[S]
(x-axis) plot in the space below. Calculate the KM and
Vmax values.
c) Calculate the...
The value of Km for the shown data for a hexokinase-catalyzed reaction is with the unit...
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...
Need help with number 13! I already asked about number
12. The inverse velocity and inverse substrate concentration relationship for an enzyme-catalyzed reaction is given below V Vmax Vmax S For the hydration of CO2 catalyzed by carbonic anhydrase, it was determined experimentally that (dm s mol 4023.9+ 39.934 at a total enzyme IS] concentration of 2.32 × 10-y mol-dm- What is the value of the Michaelis constant KM for this enzymatic reaction? (B). 9.92x103 mol dm3 (D). 100.8 mol...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
The following data were recorded for the enzyme-catalyzed reaction. Substrate concentration (M) 6.25 x 100 7.50 x 10 1.00 x 10-4 1.00 x 10-3 Reaction velocity (nM/min) 15 56 60 75 (1) Estimate Km and Vmax- (2) What would V be at S=2.5 x 10-5 ?
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...
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) 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
(15 points) The following data is for a reaction
catalyzed by tyrosine monoxygenase:
Substrate
Concentration
(mol/L)
Initial Velocity (mM/min)
1.5
0.66
1.2
0.65
0.81
0.45
0.65
0.39
0.49
0.32
0.27
0.21
a) Plot the velocity (y-axis) versus substrate
concentration [S] (x-axis) curve and insert/draw the graph in the
space below. What are the approximate KM and
Vmax values?
b) Construct a 1/v (y-axis) versus 1/[S]
(x-axis) plot in the space below. Calculate the KM and
Vmax values.
c) Calculate the...
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...
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