8. The initial rate for an enzyme-catalyzed reaction has been deter mined at a number of substrate concentrations. Data are as follows: (Sl (pmol/L) (pmol/L) min) 65 102 120 135 200 (a) Estimate Vmax and Ky from a direct graph of y versus (SI (these data are plotted in Figure 11.246). Do you find difficulties in get- ting clear answers? (b) Now use a Lineweaver-Burk plot to analyze the same data. Does this work better?
Homework Answers
| [S] u.mol /L | V( u.mol/L)/min | 1/[S] (L/u.mol) | 1/[V] (L.min/u.mol) |
|---|---|---|---|
| 5 | 22 | 0.2 | 0.045 |
| 10 | 39 | 0.1 | 0.025 |
| 20 | 65 |
0.05 |
0.015 |
| 50 | 102 | 0.02 | 0.009 |
| 100 | 120 | 0.01 | 0.008 |
| 200 | 135 |
0.005 |
0.007 |
A) [S] vs [ V] plot.
![Es] Vs CV] plot ax 125 00 50,(02) 구5 2 2 5) km2a.5 00 (25 00 50 eSI s1](http://img.homeworklib.com/questions/23f9d810-455a-11eb-933e-f9a3771e9d87.png?x-oss-process=image/resize,w_560)
Vmax = 135
Km= 22.5
There is no difficulties in getting clear answer.
B)LB plot
This plot does not work
better. Right from scale of the graph, plotting, and obtaining
1/Vmax and 1/Km values, everything is difficult.we cannot obtain
result using Lineweaver Burk plot.
Add Answer to:
8. The initial rate for an enzyme-catalyzed reaction has been
deter mined at a number of...
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number...
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are given below: 5 27 23 65 1. Estimate V and K from a Michaelis-Menten graph of V versus [S] 2. Use a Lineweaver-Burk plot to analyze the same data. a. Determine V and Ka from the Lineweaver-Burk BONUS: If the total enzyme concentration was I nmol/L, what is K?
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction...
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...
Smol-L R mol L min) 10.0 20.0 The data in the table was collected for a...
Smol-L R mol L min) 10.0 20.0 The data in the table was collected for a certain enzyme-catalyzed reaction. Use these data to determine the maximum rate of the enzyme (Rmax), often called the maximum velocity (Vmax), and the Michaelis-Menten constant of the enzyme (KM). If you were to plot this data to graphically determine Rmax and Ky using a Lineweaver-Burk plot, what would you plot? If you would use the original data in the table.er original value for your...
The following data has been obtained for an enzyme-catalyzed reaction with two different initial enzyme concentrations...
The following data has been obtained for an enzyme-catalyzed reaction with two different initial enzyme concentrations of 0.025g/L and 0.015g/L. V (g/L.min) [S] (g/L) Eo = 0.025g/L Ep = 0.015g/L 56.8 1.75 1.05 28.4 1.58 0.97 19.1 1.47 0.89 14.3 1.38 0.83 11.4 1.31 0.77 9.4 1.22 0.73 8.2 1.15 0.69 7.1 1.08 0.66 (a) Using the Lineweaver-Burke plot, determine Km and Vm for Eo = 0.025g/L (b) Using the Lineweaver-Burke plot, determine Km and Vm for Ep = 0.015g/L...
The following chart shows the data for the oxidation of a substrate to enzyme. The reaction...
The following chart shows the data for the oxidation of a substrate to enzyme. The reaction is followed by monitoring the change in absorbance at 540nm. Create a Michaelis-Menten plot and a Lineweaver-Burk plot. Determine from each plot the KM and Vmax. [S] (mM) 0.3 0.6 1.2 4.8 Rate (ΔAbs/min) 0.020 0.035 0.048 0.081
1. The turnover number for an enzyme is known to be 5000 min. From the following set of data, calculate the Km, Vma...
1. The turnover number for an enzyme is known to be 5000 min. From the following set of data, calculate the Km, Vmax and the amount of enzyme present in this experiment. Use excel to obtain the lineweaver burk plot. Substrate concentration (MM) 1 Initial velocity (umol/min) 167 250 334 376 498 499 100 1,000
(15 points) The following data is for a reaction catalyzed by tyrosine monoxygenase: Substrate Concentration (mol/L) ...
(15 points) The following data is for a reaction
catalyzed by tyrosine monoxygenase:
Substrate
Concentration
(mol/L)
Initial Velocity (mM/min)
1.5
0.66
1.2
0.65
0.81
0.45
0.65
0.39
0.49
0.32
0.27
0.21
a) Plot the velocity (y-axis) versus substrate
concentration [S] (x-axis) curve and insert/draw the graph in the
space below. What are the approximate KM and
Vmax values?
b) Construct a 1/v (y-axis) versus 1/[S]
(x-axis) plot in the space below. Calculate the KM and
Vmax values.
c) Calculate the...
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed react...
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. S Where v is the velocity or rate, Vmax is the maximum velocity, Km is the +IST Michaelis- Menten constant, and I5 s the substrate concentration. K + S v (uM/min) a) A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (Vo) at different substrate concentrations ([S]) 300 Vmax 250 1/2 Vmax First, move the line labeled "Vmax to a...
need B C and D done please please please help!!! 1. You measure the initial rate...
need B C and D done please please please help!!!
1. You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: V. (-) Inhibitor (mm/min) (+) Inhibitor (mM/min) 17 [S] (MM) 0.0001 0.0002 0.0005 0.001 0.002 Please submit calculations and graph for full credit! Note: You are required to use Excel to generate the Lineweaver-Burk plot (a) (10 points) Create a Lineweaver-Burk...
Initial rates of an enzyme-catalyzed reaction for various substrate concentrations are listed in the table below....
Initial rates of an enzyme-catalyzed reaction for various substrate concentrations are listed in the table below. From this data determine Km and Vm S(M)v (HM/min) 4.1x103 9.5x104 5.2x104 1.03x104 4.9x10-5 1.06x10 5.1x10-6 173 125 106 80 67 43
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction has been determined at a number of substrate concentrations. Data are given below: 5 27 23 65 1. Estimate V and K from a Michaelis-Menten graph of V versus [S] 2. Use a Lineweaver-Burk plot to analyze the same data. a. Determine V and Ka from the Lineweaver-Burk BONUS: If the total enzyme concentration was I nmol/L, what is K?
Enzyme Kinetics Problem The initial rate for an enzyme-catalyzed reaction...
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...
Smol-L R mol L min) 10.0 20.0 The data in the table was collected for a certain enzyme-catalyzed reaction. Use these data to determine the maximum rate of the enzyme (Rmax), often called the maximum velocity (Vmax), and the Michaelis-Menten constant of the enzyme (KM). If you were to plot this data to graphically determine Rmax and Ky using a Lineweaver-Burk plot, what would you plot? If you would use the original data in the table.er original value for your...
The following data has been obtained for an enzyme-catalyzed reaction with two different initial enzyme concentrations of 0.025g/L and 0.015g/L. V (g/L.min) [S] (g/L) Eo = 0.025g/L Ep = 0.015g/L 56.8 1.75 1.05 28.4 1.58 0.97 19.1 1.47 0.89 14.3 1.38 0.83 11.4 1.31 0.77 9.4 1.22 0.73 8.2 1.15 0.69 7.1 1.08 0.66 (a) Using the Lineweaver-Burke plot, determine Km and Vm for Eo = 0.025g/L (b) Using the Lineweaver-Burke plot, determine Km and Vm for Ep = 0.015g/L...
1. The turnover number for an enzyme is known to be 5000 min. From the following set of data, calculate the Km, Vmax and the amount of enzyme present in this experiment. Use excel to obtain the lineweaver burk plot. Substrate concentration (MM) 1 Initial velocity (umol/min) 167 250 334 376 498 499 100 1,000
(15 points) The following data is for a reaction
catalyzed by tyrosine monoxygenase:
Substrate
Concentration
(mol/L)
Initial Velocity (mM/min)
1.5
0.66
1.2
0.65
0.81
0.45
0.65
0.39
0.49
0.32
0.27
0.21
a) Plot the velocity (y-axis) versus substrate
concentration [S] (x-axis) curve and insert/draw the graph in the
space below. What are the approximate KM and
Vmax values?
b) Construct a 1/v (y-axis) versus 1/[S]
(x-axis) plot in the space below. Calculate the KM and
Vmax values.
c) Calculate the...
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. S Where v is the velocity or rate, Vmax is the maximum velocity, Km is the +IST Michaelis- Menten constant, and I5 s the substrate concentration. K + S v (uM/min) a) A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (Vo) at different substrate concentrations ([S]) 300 Vmax 250 1/2 Vmax First, move the line labeled "Vmax to a...
need B C and D done please please please help!!!
1. You measure the initial rate of an enzyme reaction as a function of substrate concentration in the presence and absence of an inhibitor. The following data was obtained: V. (-) Inhibitor (mm/min) (+) Inhibitor (mM/min) 17 [S] (MM) 0.0001 0.0002 0.0005 0.001 0.002 Please submit calculations and graph for full credit! Note: You are required to use Excel to generate the Lineweaver-Burk plot (a) (10 points) Create a Lineweaver-Burk...
Initial rates of an enzyme-catalyzed reaction for various substrate concentrations are listed in the table below. From this data determine Km and Vm S(M)v (HM/min) 4.1x103 9.5x104 5.2x104 1.03x104 4.9x10-5 1.06x10 5.1x10-6 173 125 106 80 67 43
Most questions answered within 3 hours.
-
Which statement is always true: The total energy of a closed
system...
A) is always equally...
asked 7 minutes ago -
find the critical value associated with a right sided hypothesis of
the mean using a sample...
asked 2 hours ago -
Which of the following statements is true with respect to a
simple linear regression model?
a....
asked 2 hours ago -
The energy required to remove an electron from a surface of a
solid element is called...
asked 4 hours ago -
How would you train your employees to avoid risks of using
mobile devices?
asked 4 hours ago -
Assume Kw = 1.01 ✕ 10−14
For pure water, we can calculate [H3O+ ] = [OH...
asked 5 hours ago -
Suppose that on a temperature scale X, water boils at 203.0°X
and freezes at -105.7°X. What...
asked 6 hours ago -
BaS crystallizes in a cubic unit cell with S2- ions on each
corner and each face....
asked 6 hours ago -
A. 0≤P(Oi)≤10≤P(Oi)≤1 for each i
B. P(Oi)≤0P(Oi)≤0
C. P(Oi)=1+P(OCi)P(Oi)=1+P(OiC)
D. P(Oi)≥1P(Oi)≥1
If an experiment consists of...
asked 8 hours ago -
A battery has an emf of 9.20V and an internal resistance of 1.20
ohm. a)What resistance...
asked 8 hours ago -
The area of an elastic circular loop decreases at a constant
rate, dA/dt = −6.60×10−3 m2/s...
asked 9 hours ago -
The denaturation of proteins can be described by the
equilibrium
F⇌U
where F and U represent...
asked 11 hours ago