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
Homework Answers
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Vmax is a poor metric for comparing enzyme efficiencies
because:
it is independent of the total...
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.
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...
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...
Vmax II. Enzyme Kinetics 1. Vocabulary - match the term on the left with the definition...
Vmax II. Enzyme Kinetics 1. Vocabulary - match the term on the left with the definition on the right (each used only once) keat a. Concentration of inhibitor where the velocity is the maximum under a given set of conditions. Allostery b. Changes in active site properties through ligand binding to another site. K c. Rate of an enzyme reaction under a given set of conditions. Hill coefficent d. Maximum rate for an enzyme under a given set of conditions....
41. You want to determine the initial velocity (Vo) of an enzyme, which has a Vmax...
41. You want to determine the initial velocity (Vo) of an enzyme, which has a Vmax of 0.3??/s and you are using an enzyme concentration of 50mM. The concentration of substrate in the reaction is 8 times greater than the Km. Which value below is the correct initial velocity A. 0.09 HM/s B. 0.27 ??/s C. 0.04 HM/s D. 1??/s E. 0.7 ??/s
Question 5 (1 point) Saved Suppose a cell that had a total enzyme concentration of 1,...
Question 5 (1 point) Saved Suppose a cell that had a total enzyme concentration of 1, suddenly reduced that concentration to 0.5; everything else in the cell was constant. Choose all of the values from the list below that must change as a result of the change in enzyme concentration. 1) Km 2) Vmax 3) substrate concentration 4) reaction velocity
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...
You have an inhibitor for an enzyme that you are studying. The concentration of inhibitor used is...
You have an inhibitor for an enzyme that you are studying. The concentration of inhibitor used is 5.50 µM. The following data was collected for the non-inhibited reaction as well as the reaction that was inhibited. mmol/(mL min) mmol/(mL min) mM Substrate Vo Substrate Vo + Inhibitor 0.200 5.000 3.751 0.400 7.500 4.998 0.800 10.000 5.995 1.000 10.700 6.173 2.000 12.500 6.807 4.000 13.600 7.143 a. Plot this data using Excel or a graphing program. Make sure you give your graph has a...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence and absence of 3 mM inhibitor Z. The initial velocity data obtained are shown below: [S] (mmoles liter) v (mmoles"litermin) no inhibitor inhibitor Z 1.25 1.67 2.50 5.00 10.0 1.72 2.04 2.63 3.33 4.17 0.98 1.17 1.47 1.96 2.38 (4 pts) Estimat e Vmax and Kw in the presence and absence of inhibitor using the Michaelis Menton curve-fitting program on Kaleidagraph (see lab manual)....
i need help with part two PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence...
i
need help with part two
PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence of inhibitor A. The initial rate is given as a function of substrate concentration in the following table. [S] (MM) * Velocity in substrate only y (mM/min) .25 1.72 58 ,598 r.60 2.04 .44 50 A 2.63 238 5.00 .2 3.33 10.00 4.17 4 Velocity in substrate + S inhibitor A (MM/min) 0.98 1.02 | 1.17 . 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...
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...
Vmax II. Enzyme Kinetics 1. Vocabulary - match the term on the left with the definition on the right (each used only once) keat a. Concentration of inhibitor where the velocity is the maximum under a given set of conditions. Allostery b. Changes in active site properties through ligand binding to another site. K c. Rate of an enzyme reaction under a given set of conditions. Hill coefficent d. Maximum rate for an enzyme under a given set of conditions....
41. You want to determine the initial velocity (Vo) of an enzyme, which has a Vmax of 0.3??/s and you are using an enzyme concentration of 50mM. The concentration of substrate in the reaction is 8 times greater than the Km. Which value below is the correct initial velocity A. 0.09 HM/s B. 0.27 ??/s C. 0.04 HM/s D. 1??/s E. 0.7 ??/s
Question 5 (1 point) Saved Suppose a cell that had a total enzyme concentration of 1, suddenly reduced that concentration to 0.5; everything else in the cell was constant. Choose all of the values from the list below that must change as a result of the change in enzyme concentration. 1) Km 2) Vmax 3) substrate concentration 4) reaction velocity
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...
1. The kinetics of an enzyme was examined at various substrate concentrations in both the presence and absence of 3 mM inhibitor Z. The initial velocity data obtained are shown below: [S] (mmoles liter) v (mmoles"litermin) no inhibitor inhibitor Z 1.25 1.67 2.50 5.00 10.0 1.72 2.04 2.63 3.33 4.17 0.98 1.17 1.47 1.96 2.38 (4 pts) Estimat e Vmax and Kw in the presence and absence of inhibitor using the Michaelis Menton curve-fitting program on Kaleidagraph (see lab manual)....
i
need help with part two
PART TWO 1) The steady-state kinetics of an enzyme is studied in the absence and presence of inhibitor A. The initial rate is given as a function of substrate concentration in the following table. [S] (MM) * Velocity in substrate only y (mM/min) .25 1.72 58 ,598 r.60 2.04 .44 50 A 2.63 238 5.00 .2 3.33 10.00 4.17 4 Velocity in substrate + S inhibitor A (MM/min) 0.98 1.02 | 1.17 . 5...
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