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![t = km 1 + 1 ud Y Vmax [s] max kms Michaelis menten Constant Vmaxs is the maximum reaction a velocity from the graph =1258 +](http://img.homeworklib.com/questions/15f70680-1fc1-11ec-9079-cd39a7d19d89.png?x-oss-process=image/resize,w_560)
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The activity of an enzyme was tested in the presence of a mixed type of inhibitor....
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
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...
For a report, after plotting the lineweaver-burk plot for a protease enzyme with and without inhibitor....
For a report, after plotting the lineweaver-burk plot for a protease enzyme with and without inhibitor. It shows that the km value increases in the presence of inhibitor and Vmax decreases. what type of inhibition is it? The inhibitor is an azide.
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
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...
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
please explain and answere Question 11 (1 point) A competitive inhibitor has [1] = 269 uM....
please explain and answere
Question 11 (1 point) A competitive inhibitor has [1] = 269 uM. The y-intercept for the Lineweaver-Burke plot is 9900 s*um 1. The x-intercept for the Lineweaver-Burke plot in the presence of the inhibitor is -0.0040 MM 1. Km for the uninhibited is 32 uM. Calculate the Ki for the inhibitor in uM. Round your answer to the nearest whole number (i.e. if you calculated 10.03, input your answer as 10) Your Answer: Your Answer
A class conducts an enzyme kinetics experiment using the digestive enzyme, trypsin and an unknown inhibior....
A class conducts an enzyme kinetics experiment using the
digestive enzyme, trypsin and an unknown inhibior. They generate
the two curves below. According this data, what type of inhibitor
did the students use?
1. Competitive 2. Non- Competitive
In the same Lineweaver-Burke plot from question above, what is
the approximate value of Vmax?
1/4
100
0.01
Vmax cannot be determined from this plot.
An experiment was performed to determine the effects of an inhibitor on the breakdown of glycogen...
An experiment was performed to determine the effects of an inhibitor on the breakdown of glycogen by an enzyme. In an accompanying experiment, the inhibitor was added to the glycogen-enzyme suspension and reacted using the same experimental conditions. The data obtained from these experiments is tabulated below. Draw the Michaelis-Menten and Lineweaver-Burke plots of these data. Determine the form of inhibition observed from these results and explain your rationale for this form. Determine the values for K_m and V_max from...
The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme...
The following observations come from Lineweaver-Burke plots, based on kinetic data generated from a Michaelis/Menton-type enzyme (E) that catalyzes the hydrolysis of a peptide substrate (S). All data were generated in the presence of 18.0 μM total enzyme. The enzyme-catalyzed reaction has a Km of 3.00 μM and a Vmax of 2.00 μM/sec. The enzyme-catalyzed reaction in the presence of 15.0 μM of Inhibitor A has an apparent Km of 2.25 μM and an apparent Vmax of 1.50 μM/sec. The...
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
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...
please explain and answere
Question 11 (1 point) A competitive inhibitor has [1] = 269 uM. The y-intercept for the Lineweaver-Burke plot is 9900 s*um 1. The x-intercept for the Lineweaver-Burke plot in the presence of the inhibitor is -0.0040 MM 1. Km for the uninhibited is 32 uM. Calculate the Ki for the inhibitor in uM. Round your answer to the nearest whole number (i.e. if you calculated 10.03, input your answer as 10) Your Answer: Your Answer
A class conducts an enzyme kinetics experiment using the
digestive enzyme, trypsin and an unknown inhibior. They generate
the two curves below. According this data, what type of inhibitor
did the students use?
1. Competitive 2. Non- Competitive
In the same Lineweaver-Burke plot from question above, what is
the approximate value of Vmax?
1/4
100
0.01
Vmax cannot be determined from this plot.
An experiment was performed to determine the effects of an inhibitor on the breakdown of glycogen by an enzyme. In an accompanying experiment, the inhibitor was added to the glycogen-enzyme suspension and reacted using the same experimental conditions. The data obtained from these experiments is tabulated below. Draw the Michaelis-Menten and Lineweaver-Burke plots of these data. Determine the form of inhibition observed from these results and explain your rationale for this form. Determine the values for K_m and V_max from...
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