Why is the V max of an enzyme-catalyzed reaction the same in the presence of a...
Why is the V max of an enzyme-catalyzed reaction the same in the presence of a competitive inhibitor as it is in the absence of one?
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Why is the V max of an enzyme-catalyzed reaction the same in the
presence of a...
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
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
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...
20.8 2) Consider the following data for an enzyme-catalyzed hydrolysis reaction in the presence and absence...
20.8 2) Consider the following data for an enzyme-catalyzed hydrolysis reaction in the presence and absence of inhibitor I using a Michaelis-Menten plot, determine Kn for both inhibited and uninhibited reactions. What kind of inhibition is this? [Substrate)(M) vo (umol/min) Vos (moles/min) 6x106 4.2 1x105 29 5.8 2x105 6x109 13.6 1.8x10* 16.2
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...
Please show me how to solve these and I'll give thumbs up. Thank you! Question 6...
Please show me how to solve these and I'll give thumbs up.
Thank you!
Question 6 O out of 10 points 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? Question 7 O...
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...
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equatio...
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equation as shown below: V0 = (-Km) V0 / [S] + Vmax a). Please derive the Eadie-Hofstee equation starting from the Michaelis-Menten equation. b). The Vmax and Km of the enzyme catalyzed reaction can be derived from a plot of V0 versus V0/[S]. Please draw one of these plots and explain how do you use it to derive Vmax and Km. c). Please draw a...
8. A chemist obtains the following Lineweaver-Burk plots for an enzyme catalyzed reaction in the ...
Pysical Chemistry! Please show all work thank you.
8. A chemist obtains the following Lineweaver-Burk plots for an enzyme catalyzed reaction in the absence and presence of two different inhibitors, A and B. The linear fit for no inhibition is 302.61.96 x 105 .0 x 10 2.5 x 10 2.0 x 10 1.5x 10 1.0 x10 The linear fit for inhibitor A is: 757.82.03 x 105 No inhibitor And the linear fit for inhibitor B is 50 к 10°- 1015.35.95...
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
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...
20.8 2) Consider the following data for an enzyme-catalyzed hydrolysis reaction in the presence and absence of inhibitor I using a Michaelis-Menten plot, determine Kn for both inhibited and uninhibited reactions. What kind of inhibition is this? [Substrate)(M) vo (umol/min) Vos (moles/min) 6x106 4.2 1x105 29 5.8 2x105 6x109 13.6 1.8x10* 16.2
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...
Please show me how to solve these and I'll give thumbs up.
Thank you!
Question 6 O out of 10 points 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? Question 7 O...
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...
Pysical Chemistry! Please show all work thank you.
8. A chemist obtains the following Lineweaver-Burk plots for an enzyme catalyzed reaction in the absence and presence of two different inhibitors, A and B. The linear fit for no inhibition is 302.61.96 x 105 .0 x 10 2.5 x 10 2.0 x 10 1.5x 10 1.0 x10 The linear fit for inhibitor A is: 757.82.03 x 105 No inhibitor And the linear fit for inhibitor B is 50 к 10°- 1015.35.95...
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