![Question 11 (1 point) A competitive inhibitor has [1] = 269 uM. The y-intercept for the Lineweaver-Burke plot is 9900 s*um 1.](http://img.homeworklib.com/questions/50e40210-069d-11ec-be1e-b14ac84300b1.png?x-oss-process=image/resize,w_560)
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![peat Lineweaner -Burk y t innistar no inhibion Km Vmax [5] on Vmax son Y intercept 1 V max intercept 2 KM so I = 99 oostumi s](http://img.homeworklib.com/questions/7151f410-069d-11ec-990f-6942bb0c72c9.png?x-oss-process=image/resize,w_560)
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Question 11 (1 point) A competitive inhibitor has [1] = 269 uM....
Biochemistry inhibitors! Pls answer 1 through 11 For each of the following items, indicate whether the...
Biochemistry inhibitors! Pls answer 1 through 11
For each of the following items, indicate whether the item pertains to: • Competitive inhibitor . Uncompetitive inhibitor • Noncompetitive inhibitor • Noncompetitive activator • None of the above Choose only one of the above for each item. 1. Binds to the enzyme-substrate complex only 2. Prevents substrate from binding enzyme 3. Forms inactive El or inactive ESI complex 4. When present, Vmax increases 5. When present, Vmax increases and Km decreases 6....
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...
please graph all 3 lines and explain the vmax&km How to: Lineweaver Burke 1. The following...
please graph all 3 lines and explain the
vmax&km
How to: Lineweaver Burke 1. The following data was determined for an enzyme in the absence of an inhibitor and in the presence of two different inhibitors (V2 and V3). Determine the V. and K for the enzyme (1) Plot the data and determine the type of inhibition for each inhibitor (S) mm 1 V2 4.3 5.5 V1 12 20 29 2 relliate 150b
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...
Can help me with these questions please. 30. Sphingosine-1-phosphate (S1P) is important for cell survival. The...
Can help me with these questions please. 30. Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below. Sphingosine (uM) vo (mg /min) vo (mg /min) with inhibitor 2.5 32.3 8.5 3.5 40 11.5 5.0 50.8 14.6 10 72...
Sphingosine 1-phophate (SPP) is important for cell survival. The synthesis of SPP from sphingosine and ATP...
Sphingosine 1-phophate (SPP) is important for cell survival. The
synthesis of SPP from sphingosine and ATP is catalyzed by the
enzyme sphingosine kinase. An understanding of the kinetics of the
sphingosine kinase reaction may be important in the development of
drugs to treat cancer. The velocity of the spingosine kinase
reaction was measured inthe presence and absence of
threo-sphingosine, a sterioisomer of sphingosine that inhibits the
enzyme. The results are next.
Contruct a lineweaver-Burk plot to answer the following
questions:...
i need help with all question 5 please! thank you Question 5: Use the data below...
i need help with all question 5 please! thank you
Question 5: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo (UM/s) a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest [S]? c) Using your Vmax estimate, calculate ! Vmax, and using your curve, estimate Km. 1/[S] M 8 1/VO (s/UM) 3.85E-03 [S]...
only need answer for question d and e. thanks 2. Captopril was the first of a...
only need answer for question d and e. thanks
2. Captopril was the first of a class of blood pressure lowering drugs that work by reversibly inhibiting Angiotension-converting enzyme (ACE). Later to the market was Lisinopril. This class of drugs is the fifth most prescribed, approaching 200 million prescriptions per year in the US alone. ACE inhibitors work by preventing the proteolytic cleavage of angiotensin I by ACE to create its active form angiotensin II, which binds to receptors in...
Biochemistry inhibitors! Pls answer 1 through 11
For each of the following items, indicate whether the item pertains to: • Competitive inhibitor . Uncompetitive inhibitor • Noncompetitive inhibitor • Noncompetitive activator • None of the above Choose only one of the above for each item. 1. Binds to the enzyme-substrate complex only 2. Prevents substrate from binding enzyme 3. Forms inactive El or inactive ESI complex 4. When present, Vmax increases 5. When present, Vmax increases and Km decreases 6....
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...
please graph all 3 lines and explain the
vmax&km
How to: Lineweaver Burke 1. The following data was determined for an enzyme in the absence of an inhibitor and in the presence of two different inhibitors (V2 and V3). Determine the V. and K for the enzyme (1) Plot the data and determine the type of inhibition for each inhibitor (S) mm 1 V2 4.3 5.5 V1 12 20 29 2 relliate 150b
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...
Sphingosine 1-phophate (SPP) is important for cell survival. The
synthesis of SPP from sphingosine and ATP is catalyzed by the
enzyme sphingosine kinase. An understanding of the kinetics of the
sphingosine kinase reaction may be important in the development of
drugs to treat cancer. The velocity of the spingosine kinase
reaction was measured inthe presence and absence of
threo-sphingosine, a sterioisomer of sphingosine that inhibits the
enzyme. The results are next.
Contruct a lineweaver-Burk plot to answer the following
questions:...
i need help with all question 5 please! thank you
Question 5: Use the data below to construct a Michaelis-Menton curve of velocity vs. [S]. This is quite easy to do in Excel. Vo (UM/s) a) Estimate Vmax from your curve. b) Describe any difficulty you have in completing part (a). Is the enzyme saturated at the highest [S]? c) Using your Vmax estimate, calculate ! Vmax, and using your curve, estimate Km. 1/[S] M 8 1/VO (s/UM) 3.85E-03 [S]...
only need answer for question d and e. thanks
2. Captopril was the first of a class of blood pressure lowering drugs that work by reversibly inhibiting Angiotension-converting enzyme (ACE). Later to the market was Lisinopril. This class of drugs is the fifth most prescribed, approaching 200 million prescriptions per year in the US alone. ACE inhibitors work by preventing the proteolytic cleavage of angiotensin I by ACE to create its active form angiotensin II, which binds to receptors in...
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