How do competitive inhibitors affect the KM and Vmax of an enzyme? Draw a plot of...
How do competitive inhibitors affect the KM and Vmax of an enzyme? Draw a plot of velocity as a function of substrate concentration, both with and without inhibitor added.
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How do competitive inhibitors affect the KM and Vmax of an
enzyme? Draw a plot of...
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as...
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as a function of substrate concentration; label both axes. Write the associated Michaelis-Menton equation and show the location of Km and Vmax on your graph. b. Draw a second graph showing the classic Lineweaver-Burk plot; label both axes. Show the location of Km and Vmax on your graph. Discuss which plot is the most useful to determine Vmax. Draw a second line on each graph...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
Vmax is a poor metric for comparing enzyme efficiencies because: it is independent of the total...
Vmax is a poor metric for comparing enzyme efficiencies because: it is independent of the total enzyme concentration b. it varies as a function of the Km value of the substrate it changes as a result of using competitive inhibitor d. the total ezymes concentration affects the value of Vmax it requires measuring enzyme velocity
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...
biochemistry: how do noncompetitive, mixed, and uncompetitive inhibitors affect Km and Vmax?
biochemistry: how do noncompetitive, mixed, and uncompetitive inhibitors affect Km and Vmax?
b. Look at the graph below of how a competitive inhibitor affects the kinetics of an...
b. Look at the graph below of how a competitive inhibitor affects the kinetics of an enzyme C. Rate of reaction is the Vmax of the enzyme affected? Why or why not: explain in terms of substrate concentration and enzyme active site saturation) Without inhibitor With competitive inhibitor d. is Vmax/2 affected? Why or why not: explain in terms of Vmax. Substrate concentration e. Is Km affected? Explain in terms of the active site. Hint a competitive inhibitor is competing...
How do I calculate the apparent vmax? 16. At right is a graph obtained from a...
How do I calculate the apparent vmax?
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 M/s. a) What is the KM? 5 4.5 4 3.5 3 2.5 2 1.5 KM: 3mm ve (MM/s) 1 0.5 0 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the...
a. An enzyme has a Vmax of 100 umol/min and a Km of 40 uM. When...
a. An enzyme has a Vmax of 100 umol/min and a Km of 40 uM. When substrate concentration is 40 uM what is the initial reaction rate? b. An enzyme with a Vmax of 100 umol/minute and a Km of 10 uM was reacted with a irreversible active site specific inhibitor. After reaction with the inhibitor, the enzyme was assayed using a 2 mM concentration of substrate, and it gave a reaction rate of 20 umol/min. What percentage of the...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. 5 4.5 4 a) What is the KM? KM: v. (mM/s) 3.5 3 2.5 2 1.5 1 0.5 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. a) What is the KM? 5 4.5 4 3.5 3 2.5 2 KM: 3mm V. (mM/s) 1.5 1 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
1. MICHAELIS-MENTON-(REQUIRED) a. Draw a simple graph, showing the classic Michaelis-Menton plot of enzyme activity as a function of substrate concentration; label both axes. Write the associated Michaelis-Menton equation and show the location of Km and Vmax on your graph. b. Draw a second graph showing the classic Lineweaver-Burk plot; label both axes. Show the location of Km and Vmax on your graph. Discuss which plot is the most useful to determine Vmax. Draw a second line on each graph...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
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...
b. Look at the graph below of how a competitive inhibitor affects the kinetics of an enzyme C. Rate of reaction is the Vmax of the enzyme affected? Why or why not: explain in terms of substrate concentration and enzyme active site saturation) Without inhibitor With competitive inhibitor d. is Vmax/2 affected? Why or why not: explain in terms of Vmax. Substrate concentration e. Is Km affected? Explain in terms of the active site. Hint a competitive inhibitor is competing...
How do I calculate the apparent vmax?
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 M/s. a) What is the KM? 5 4.5 4 3.5 3 2.5 2 1.5 KM: 3mm ve (MM/s) 1 0.5 0 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. 5 4.5 4 a) What is the KM? KM: v. (mM/s) 3.5 3 2.5 2 1.5 1 0.5 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. a) What is the KM? 5 4.5 4 3.5 3 2.5 2 KM: 3mm V. (mM/s) 1.5 1 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
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