On this plot, the slope is [– Km or: Vmaximum or Vmaximum" -] and the y-intercept is (-- or: Km or: V mazimum´ Ibuprofen [increases/decreases/does not change] Km and maximum (increases/decreases/does not change] Vmax and is thus a [competitive/uncompetitive/noncompetitive] inhibitor of cyclooxygenase.
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![• Ibuprofen
Ibuprolen
1/(S)
Km
On this plot, the slope is [--
-] and the y-intercept is
Vmaximum"
or
or
Vтaximum
Km
or
Vmaximum
1
or
Vmaximum
Ibuprofen [increases/decreases/does not change] Km and
Km
(increases/decreases/does not change] Vmax and is thus a
[competitive/uncompetitive/noncompetitive] inhibitor of cyclooxygenase.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Facf7f7d4-0a2e-4492-8754-e1a4249f75ff%2F396f9114-8e4b-42ff-8f22-77c4374471f2%2Fnqd9fml_processed.png&w=3840&q=75)
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- A biochemst wants to dtermine the effect of inhibitor on a certain enzyme. See attached data. Using linaer regression analysis, determine the values of Vmax and Km of the enzyme in the absence of an inhibitor 1. y- int ( up to 5 decimal places) 2. slope 3. Vmax 4. Km Using linear regression analysis determine the values of Vmax and Km of the enzyme in the presence of inhibitor 1. y- int ( up to 5 decimal places) 2. slope 3. Vmax 4. KmIf the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme inhibitor is inhibitor reversible or irreversible? And why?What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is impact of the lower V max on the amount of product formed ? If the lower value of black resulting in the new plot (red curve) is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible ? And why?
- The Lineweaver-Burke plots of a reaction without inhibitor and one with non-competitive inhibitor will have the same 1. Vmax2. Km3. Km/Vmax4. 1/VmaxUsing the attachment, Answer the following questions: Prepare a double reciprocal plot with all three experiments (lines) on the same graph. Use your graph, and then answer items 2, 3, and 4 below. 1. Calculate the Vmax or apparent Vmax for all three sets of data. Likewise, calculate the Km or apparent Km for each set. 2. For Inhibitor X, what is the mode/type of inhibition? 3. For Inhibitor Z, what is the mode/type of inhibition? By comparison of the apparent Vmax to the control Vmax, what is the value of α’, as defined in class? If Ki’ = 10 mM for this inhibitor, then what must the inhibitor concentration [Z] be?How do we calculate Ki of an inhibitor? Also, is Kapp the same as Km or does Kapp involve more variables?
- You are saying that the inhibitor is competitive inhibitor. But according to data Vmax for reaction (with no inhibitor) is 4,17mM/min and Vmax for reaction (with inhibitor)=2,31mM/min. Then you show that Km for reaction with no inhibitor is 1.66. Then I calculate further for Km for reaction with inhibitor by using MM equation and I get 0,9. So both the Vmax and Km is reduced in reaction with inhibitor. That must mean the inhibitor is not competitive but non-competitive inhibitor. Or is it me that got it wrong??Use the relationships revealed by a Lineweaver-Burk plot and the table of enzyme performance to calculate the Vmax and Km of the enzyme with no inhibitor. with inhibitor A, and with inhibitor B. [S] (uM) Vo (umol/min); w/ no inhib. Vo (umol/min); w/ inhib. A Vo (umol/min); w/ inhib. B 10 6.3 5.1 4.0 40 18.4 15.8 11.8 100 29.9 27.0 19.1 150 34.7 32.0 22.2 No inhib. Vmax= Km= Inhib. A Vmax= Km= Inhib. B Vmax= Km=If the new higher KM value is 0.1 mM resulting in the new plot red curve is due to presence of enzyme inhibitor is the inhibitor reversible or irreversible?
- Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X. (inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of 0.133333333333 mM per minute when [S] = 2.0 mM) 0.20 per minute 0.50 per minute 1.0 per minute 2.0 per minute 5.0 per minuteThe following data, presented by G. Bowes and W. L. Ogre in J. Biol. Chem. (1972) 247:2171–2176, describe the relative rates of incorporation of CO2 by Rubisco under N2 and under pure O2. Decide whether O2 is a competitive or uncompetitive inhibitor.2. an enzyme-catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained. (S)[M] V (umol/min) V (+inhibitor)(umol/min) 6 x 10-6 20.8 12 1 x 10-5 29 15 2 x 10-5 45 20 6 x 10-5 67.6 24 1.8 x 10-4 87 28 plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reaction and reaction with inhibitor. Use the same graph for both plots. calculate the Km of enzyme in the reaction without inhibitor Km1 of the enzyme in the reaction with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction what kind of inhibitor was added to the enzyme-catalyzed reaction? explain your answer in terms of changes in Km and Vmax.