Draw a graph of enzyme velocity as a function of total enzyme concentration (Et) in the...
Draw a graph of enzyme velocity as a function of total enzyme concentration (Et) in the presence of infinitely high substrate concentration. Label the axes and the slope of the line.
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Draw a graph of enzyme velocity as a function of total enzyme
concentration (Et) in the...
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...
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...
The following question focuses on how the parameters regulating enzyme function might change, and how these...
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menton plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. see for instance: http://en.wikipedia.org/wiki/Carbonic_anhydrase 1 Assume that one variant has a Km of 1 µM and a different variant has a Km of 10 µM....
The graph below shows an enzyme- controlled reaction. The enzyme concentration is kept constant. At concentrations...
The graph below shows an enzyme- controlled reaction. The enzyme concentration is kept constant. At concentrations of substrate greater than X, which of the following statements is true? Rate of reaction 0 Concentration of substrate X The rate of reaction is limited by enzyme concentration. The rate of reaction tends towards zero. The substrate has an inhibitory effect. The products have an inhibitory effect.
6 The graph shows the effect of substrate concentration on the rate of an enzyme- controlled...
6 The graph shows the effect of substrate concentration on the rate of an enzyme- controlled reaction. The enzyme concentration is constant. reaction rate Which statement about the graph is correct? A Between Wand X, the substrate concentration number of enzyme molecules is limiting. Between X and Y, the number of enzyme molecules is limiting. Between X and Y, the number of substrate molecules is limiting. Between X and Y, the product concentration remains the same. Thanh in the nammanni...
The inhibitor Draw a sketch on where a(n). inhibitor binds to the enzyme: The reaction in...
The inhibitor Draw a sketch on where a(n). inhibitor binds to the enzyme: The reaction in the presence of a(n)inhibitor can be written In the Michaelis-Menten graph, the inhibited reaćtion would look this as compared tot he uninhibited reaction (label both axes and draw both curves). In the Lineweaver-Burk graph, the inhibited reaction would look like this as compared tot he uninhibited reaction (label both axes and draw both curves). inhibitor, the apparent changes of Vmax and Km are as...
how do I draw graph for this? collisions between ernzyme and substrate is tion rate. Sketch...
how do I draw graph for this?
collisions between ernzyme and substrate is tion rate. Sketch this relationship on the axes in Figure 6.5 and label both axes. Lab Topic 6: Enaymes 6-5 expected to increase the reac- Figure 6.5. Eflect of temperature on Teaction rate But heat energy has another effect in addition to speeding up the move- ment of molecules. It can also disrupt the delicate attractions between the chemical side groups of amino acids, causing the enzyme...
thank you a) Do a Michaelis-Menton plot of the enzyme assay data below. Substrate Concentration mg/mL...
thank you
a) Do a Michaelis-Menton plot of the enzyme assay data below. Substrate Concentration mg/mL Velocity umole/(min-mL) 10 15 20 31 50 75 100 125 250 330 380 437 524 612 662 678 696 713 Have the substrate concentration as the x-axis of the graph, and the velocity as the y-axis. . Use a grid line every 10 substrate concentration units, and a grid line every 20 velocity units. . In Excel, gridlines can be controlled under the Chart...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point where the enzyme is working at its maximum rate (Vmax/2), and amount of substrate needed to bind half of the active sites (Km). Label these points on the graph. Vmax represents: Vm Vmax/2 represents: Reaction velocity v Vmax 2 Km represents: Kim Substrate concentration (5)
A compound is a strong competitive inhibitor with an a = 10. The total enzyme concentration...
A compound is a strong competitive inhibitor with an a = 10. The total enzyme concentration in the reaction is 10 nM. What substrate concentration reduces the velocity to 250 nM/min, knowing that this enzyme is characterized by a specificity constant of 2.1 x 105 M-1s-1 and a kcat of 25/min?
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...
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...
The graph below shows an enzyme- controlled reaction. The enzyme concentration is kept constant. At concentrations of substrate greater than X, which of the following statements is true? Rate of reaction 0 Concentration of substrate X The rate of reaction is limited by enzyme concentration. The rate of reaction tends towards zero. The substrate has an inhibitory effect. The products have an inhibitory effect.
6 The graph shows the effect of substrate concentration on the rate of an enzyme- controlled reaction. The enzyme concentration is constant. reaction rate Which statement about the graph is correct? A Between Wand X, the substrate concentration number of enzyme molecules is limiting. Between X and Y, the number of enzyme molecules is limiting. Between X and Y, the number of substrate molecules is limiting. Between X and Y, the product concentration remains the same. Thanh in the nammanni...
The inhibitor Draw a sketch on where a(n). inhibitor binds to the enzyme: The reaction in the presence of a(n)inhibitor can be written In the Michaelis-Menten graph, the inhibited reaćtion would look this as compared tot he uninhibited reaction (label both axes and draw both curves). In the Lineweaver-Burk graph, the inhibited reaction would look like this as compared tot he uninhibited reaction (label both axes and draw both curves). inhibitor, the apparent changes of Vmax and Km are as...
how do I draw graph for this?
collisions between ernzyme and substrate is tion rate. Sketch this relationship on the axes in Figure 6.5 and label both axes. Lab Topic 6: Enaymes 6-5 expected to increase the reac- Figure 6.5. Eflect of temperature on Teaction rate But heat energy has another effect in addition to speeding up the move- ment of molecules. It can also disrupt the delicate attractions between the chemical side groups of amino acids, causing the enzyme...
thank you
a) Do a Michaelis-Menton plot of the enzyme assay data below. Substrate Concentration mg/mL Velocity umole/(min-mL) 10 15 20 31 50 75 100 125 250 330 380 437 524 612 662 678 696 713 Have the substrate concentration as the x-axis of the graph, and the velocity as the y-axis. . Use a grid line every 10 substrate concentration units, and a grid line every 20 velocity units. . In Excel, gridlines can be controlled under the Chart...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point where the enzyme is working at its maximum rate (Vmax/2), and amount of substrate needed to bind half of the active sites (Km). Label these points on the graph. Vmax represents: Vm Vmax/2 represents: Reaction velocity v Vmax 2 Km represents: Kim Substrate concentration (5)
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