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20.8 2) Consider the following data for an enzyme-catalyzed hydrolysis reaction in the presence and absence...
The kinetic data given below are for an enzyme in the absence and presence of a...
The kinetic data given below are for an enzyme in the absence and presence of a reversible inhibitor. From the data, generate both a Michaelis-Menten and Linweaver-Burk Plot for both that uninbibited and inhibited reactions. Graph both the uninhibited and inhibited data on the same plot. From these data calculate the Vmax and Km for the enzyme in absence and presence of the inhibitor. Is the inhibitor working cometitively or noncompetitively? Explain. [S], mM Vo, mM/min Vo, mM, min with...
The following data was obtained for an enzyme in the absence of an inhibitor, and in...
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...
An enzyme-catalyzed reaction to the presence of 5 nM of reversible inhibitor yields a Vmax value...
An enzyme-catalyzed reaction to the presence of 5 nM of reversible inhibitor yields a Vmax value that is 80% of the value in absence of the inhibitor. The KMvalue is unchanged. a) what type of inhibition is occurring? b) what proportion of the enzyme molecule will have bound inhibitor? c) Draw the Lineweaver-Burk (known as double-reciprocal plot) for uninhibited and inhibited reaction. SHOW ALL YOUR WORK PLEASE
You measure the initial rate of an enzyme reaction as a function of substrate concentration in...
You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: Create a Michaelis-Menten plot (inhibited and uninhibited should be on the same plot! You MUST use Excel and follow the provided instructions "Non-Linear Regression Fitting of Kinetics Data". Calculate the V_max in the presence and absence of the inhibitor. Calculate the K_m in the presence and absence of the inhibitor. What type...
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...
Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has...
Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has yielded the following data. Vi is the velocity in the presence of inhibitor, V is the velocity when run without inhibitor and [S] refers to the substrate concentration. [S] V Vi 5.00 0.29 0.16 1.25 0.27 0.15 0.45 0.23 0.13 0.22 0.19 0.10 0.13 0.14 O.08 Uncompetitive No inhibition at all O None the above ONon-competitive O Competitive
Determine the type of...
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...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor....
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor....
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed non-competitive kinetics with y- intercepts of 15s -1 and 5 s -1 in the presence and absence of the inhibitor respectively. If the inhibitor binding constant was 0.5nM, calculate [I ] used in this reaction? a. 0.135nM b. none of the above c. 0.225nM d. InM e. 0.125nM
You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: Create a Michaelis-Menten plot (inhibited and uninhibited should be on the same plot! You MUST use Excel and follow the provided instructions "Non-Linear Regression Fitting of Kinetics Data". Calculate the V_max in the presence and absence of the inhibitor. Calculate the K_m in the presence and absence of the inhibitor. What type...
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...
Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has yielded the following data. Vi is the velocity in the presence of inhibitor, V is the velocity when run without inhibitor and [S] refers to the substrate concentration. [S] V Vi 5.00 0.29 0.16 1.25 0.27 0.15 0.45 0.23 0.13 0.22 0.19 0.10 0.13 0.14 O.08 Uncompetitive No inhibition at all O None the above ONon-competitive O Competitive
Determine the type of...
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...
5) (14 marks) The following kinetic data were obtained for an enzyme in the absence of inhibitor (1), and in the presence of an inhibitor at 5 mM concentration (2). Assume[ET] is the same in each experiment. [S] (MM) (1) v(umol/mL sec) 12 (2) v(umol/mL sec) 4.3 1 8 2 4 20 29 14 21 8 35 12 40 26 a. Using a graphing program (excel or sigmaplot) construct a lineweaver burke plot representing the uninhibited reaction and the inhibited...
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed competitive kinetics with x-intercepts of -10mm -1 and -3.5mm -1 in the presence and absence of the inhibitor respectively. If the inhibitor concentration used was 2micro molar (UM), calculate KI for the inhibitor enzyme binding? a. none of the above b. 0.135nM c. 0.054nM d. 0.225nM e. 1077 nM
An enzyme catalyzed reaction was performed in the presence and in the absence of an inhibitor. The Lineweaver Burk plot showed non-competitive kinetics with y- intercepts of 15s -1 and 5 s -1 in the presence and absence of the inhibitor respectively. If the inhibitor binding constant was 0.5nM, calculate [I ] used in this reaction? a. 0.135nM b. none of the above c. 0.225nM d. InM e. 0.125nM
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