1/Vo 1/[S] with I without I d. with I with 1/vo without I 1/[S] 1/vo without I 1/[S] 3. The above graphs are lineweaver-burk plots that demonstrate how inhibitors affect Michaelis Menten enzymes. For each graph identify the type of inhibition and explain how you determined that this enzyme is kinetically demonstrating this type of inhibition.
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![1/Vo
1/[S]
with I
without I
with I
with I
1/vo
without I
*-*-
1/vo
without I
1/[S]
1/[S]
3. The above graphs are lineweaver-burk plots that demonstrate how inhibitors affect
Michaelis Menten enzymes. For each graph identify the type of inhibition and explain
how you determined that this enzyme is kinetically demonstrating this type of
inhibition.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F78ffed4c-2ff7-409d-b569-6de60b21807b%2F86cc91bf-9810-4997-beea-13983b7334f8%2Fivlqba8_processed.jpeg&w=3840&q=75)
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- (a) What are the Vmax and Km (including units) for Tigerzyme? b) What are the Vmax and Km (including units) for Tigerzyme in the presenceof the inhibitor Tar Heel? (c) What are the Vmax and Km (including units) for Tigerzyme in the presenceof the inhibitor Blue Devil?Inhibitor X exerts which of the following effects on the above enzyme (maltase)? (inhibitor X changes maltase activity to a V o of 0.10 mM per minute when [S] = 0.125 mM, and a V o of 0.25 mM per minute when [S] = 0.50 mM)Inhibitor X exerts which of the following effects on the above enzyme (lactase)? (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) pure non-competitive inhibition uncompetitive inhibition competitive inhibition all of the above none of the above
- 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?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?Refer to the figure below and answer the following questions: Legend: Blue – wild-type β-galactosidase; Red – mutant β-galactosidase _________ a. What is the optimum pH of wild type β-galactosidase? _________ b. What is the optimum temperature of mutant β-galactosidase? _________ c. Which enzyme has the greater activity at pH 7.2? _________ d. Which enzyme has the greater activity at a temperature of 42.5oC? _________ e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? _________ f. Which enzyme has greater activity if temperature increases from 40oC to 41 oC?
- Under what conditions does Km represent the true binding affinity (i.e. Kd) of the substrate to the enzyme? 1. when kcat << k-1 2. when k-1 >> k1 3. when k1 >> kcat 4. when k1 = k-1Inhibitor X exerts which of the following effects on the above enzyme (maltase)? (inhibitor X changes maltase activity to a Vo of 0.10 mM per minute when [S] = 0.125 mM, and a Vo of 0.25 mM per minute when [S] = 0.50 mM) competitive inhibition pure non-competitive inhibition uncompetitive inhibition all of the above none of the aboveBased on this graph, it appears that carboxylesterase is most active at a pH of A. 3.5B. 1.5C. 5D. 4
- What type of inhibition is being shown in the following graphs?A competitive inhibitor binds to the - active site of theenzyme - a substrate -N termininus of the enzyme -more than one of theseA 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. Km