Homework Answers
As conc. of inhibitor is necessary to calculate Ki. I have calculate upto that as inhibitor concentration is not given. Just put [I] if you have it, in the given formula you will get the answer.
![[S] mM 2 V (without I) mm/min V (with I) mm/min 1/[S] 1.43 1.08 1.11 0.74 0.77 0.45 0.48 0.26 0.22 0.11 1/V (without I) 1/V (](http://img.homeworklib.com/questions/07274b60-d960-11eb-b367-91b74e989c22.png?x-oss-process=image/resize,w_560)
![(11 Without inhibitor, 0.8096 r +0,4887 + I VESD KM Umax [s] I Unax .. KM = 0.8096 - l = 0.4887 : Vmax = 2.046 MM/min | Vuax](http://img.homeworklib.com/questions/07bd1870-d960-11eb-9e43-27eb9947f46d.png?x-oss-process=image/resize,w_560)
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8. For the hypothetical data below, determine the type of inhibition and calculate KI Substrate concentration...
Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has...
Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has yielded the following data. Vi is the velocity in the presence of inhibitor, V is the velocity when run without inhibitor and [S] refers to the substrate concentration. [S] V Vi 5.00 0.29 0.16 1.25 0.27 0.15 0.45 0.23 0.13 0.22 0.19 0.10 0.13 0.14 O.08 Uncompetitive No inhibition at all O None the above ONon-competitive O Competitive
Determine the type of...
(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...
Question 28 1 pts Determine the type of inhibition that has occurred in a first order...
Question 28 1 pts Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has yielded the following data. Vi is the velocity in the presence of inhibitor, V is the velocity when run without inhibitor and [S] refers to the substrate concentration s V 4.00 0.28 0.28 .33 0.27 0.25 0.56 0.24 0.20 0.20 0.18 0.13 0.10 0.13 0.08 O Non-competitive O Competitive O None of the above No inhibition at all...
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...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
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...
please show how to calculate the substrate concentration in the test tubes at time=zero point 3...
please show how to calculate the substrate concentration in
the test tubes at time=zero point
3 .375 0.84-0.bda 2min What is the amount of enzyme that you chose to use in Part B? Part B- Dis cusion 1. Calculate the units of enzyme activity for the varying amounts of sub- strate. Calculate the substrate concentrations in the test tubes at time = zero point. Substrate Volume (mL) L-DOPA (mM) AA479/min umol/min 0.05 0.jas 0. 10 4 0. a5 0.1 0.208...
10. The table below is the results of the study of enzymatic reaction with and without inhibitor. What type of inhibito...
10. The table below is the results of the study of enzymatic reaction with and without inhibitor. What type of inhibitor is it? Explain! Enzyme concentration in all reactions is 1 uM [Inh], μΜ S], mM 0 0.2 0.4 0.7 rate, umol/min 0 0 0 0 0 0.5 23.5 18.8 14.1 7.0 1 32.2 25.8 19.4 9.7 1.5 36.9 29.5 22.1 11.1 2.5 41.8 33.3 25.0 12.5 3.5 44 35.2 26.4 13.2
The value of Km for the shown data for a hexokinase-catalyzed reaction is with the unit...
The value of Km for the shown data for a hexokinase-catalyzed reaction is with the unit of . The value of Vmax for. the same reaction is with the unit of . Be sure to give the values with the correct number of significant figures. You might have to construct a kinetic plot. For units, choose one answer from (uM, 1/ UM, HM/second, uM x second, mM, 1/mM, second, 1/second, mM/second, mM x second) vo (mM/sec) Glucose concentration (mm) 0.10...
Please help with a-e The data below describes the synthesis of PGG2, a prostaglandin precursor molecule,...
Please help with a-e
The data below describes the synthesis of PGG2, a
prostaglandin precursor molecule, by a COX enzyme in the presence
and absence of ibuprofen. Ibuprofen has a molecular weight of 206
g/mol. (Please see photo for data chart)
a. Determine the Vmax and KM of the enzyme with no
ibuprofen.
b. Determine the Vmax and KMapparent of the enzyme in the
presence of ibuprofen.
c. Based on your answers to a and b, what type of inhibition...
Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has yielded the following data. Vi is the velocity in the presence of inhibitor, V is the velocity when run without inhibitor and [S] refers to the substrate concentration. [S] V Vi 5.00 0.29 0.16 1.25 0.27 0.15 0.45 0.23 0.13 0.22 0.19 0.10 0.13 0.14 O.08 Uncompetitive No inhibition at all O None the above ONon-competitive O Competitive
Determine the type of...
(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...
Question 28 1 pts Determine the type of inhibition that has occurred in a first order Michaelis-Menten enzyme catalyzed reaction that has yielded the following data. Vi is the velocity in the presence of inhibitor, V is the velocity when run without inhibitor and [S] refers to the substrate concentration s V 4.00 0.28 0.28 .33 0.27 0.25 0.56 0.24 0.20 0.20 0.18 0.13 0.10 0.13 0.08 O Non-competitive O Competitive O None of the above No inhibition at all...
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...
2. The table shows the kinetic data for a reaction catalyzed by an enzyme under the following conditions: in the absence of an inhibitor, and in the presence of two different inhibitors, (1) and (2) each at a concentration of 10 mM. Assume the total enzyme concentration, [Elo, is the same for all reactions and the enzyme obeys the Michaelis-Menten mechanism In the presence of presence of 10 mM inhibitor 1 inhibitor2 In the 10 mM No inhibitor mM 2.5...
please show how to calculate the substrate concentration in
the test tubes at time=zero point
3 .375 0.84-0.bda 2min What is the amount of enzyme that you chose to use in Part B? Part B- Dis cusion 1. Calculate the units of enzyme activity for the varying amounts of sub- strate. Calculate the substrate concentrations in the test tubes at time = zero point. Substrate Volume (mL) L-DOPA (mM) AA479/min umol/min 0.05 0.jas 0. 10 4 0. a5 0.1 0.208...
10. The table below is the results of the study of enzymatic reaction with and without inhibitor. What type of inhibitor is it? Explain! Enzyme concentration in all reactions is 1 uM [Inh], μΜ S], mM 0 0.2 0.4 0.7 rate, umol/min 0 0 0 0 0 0.5 23.5 18.8 14.1 7.0 1 32.2 25.8 19.4 9.7 1.5 36.9 29.5 22.1 11.1 2.5 41.8 33.3 25.0 12.5 3.5 44 35.2 26.4 13.2
The value of Km for the shown data for a hexokinase-catalyzed reaction is with the unit of . The value of Vmax for. the same reaction is with the unit of . Be sure to give the values with the correct number of significant figures. You might have to construct a kinetic plot. For units, choose one answer from (uM, 1/ UM, HM/second, uM x second, mM, 1/mM, second, 1/second, mM/second, mM x second) vo (mM/sec) Glucose concentration (mm) 0.10...
Please help with a-e
The data below describes the synthesis of PGG2, a
prostaglandin precursor molecule, by a COX enzyme in the presence
and absence of ibuprofen. Ibuprofen has a molecular weight of 206
g/mol. (Please see photo for data chart)
a. Determine the Vmax and KM of the enzyme with no
ibuprofen.
b. Determine the Vmax and KMapparent of the enzyme in the
presence of ibuprofen.
c. Based on your answers to a and b, what type of inhibition...
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