CAMPBELL BIOLOGY-MASTERINGBIOLOGY ACC.
11th Edition
ISBN: 9781323488638
Author: Pearson
Publisher: PEARSON
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Chapter 8.4, Problem 3CC
WHAT IF? Ø Malonate is an inhibitor of the enzyme succinate dehydrogenase. How would you determine whether malonate is a competitive or noncompetitive inhibitor?
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Let’s consider vmax. Recall that uncompetitive inhibitors bind to the enzyme only after thesubstate is bound.a) As the concentration of substrate increases, the fraction of enzyme bound to substrate (circleone) increases / decreases?b) Does an uncompetitive inhibitor bind more readily when the substrate concentration is low orhigh?
Explain Why and How Questions??? Give the reasons and examples!!! Add Structures too if present!!
1- Many enzyme sites for inhibition?
2- Line Weaver Burk is better than Michalis Mentin curve?
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"Yeast yields ethanol from pyruvate in two steps. Step one requires the co-enzyme __ , which is necessary for the substrate to undergo oxidative decarboxylation."
Chapter 8 Solutions
CAMPBELL BIOLOGY-MASTERINGBIOLOGY ACC.
Ch. 8.1 - MAKE CONNECTIONS How does the second law of...Ch. 8.1 - Describe the forms of energy found in an apple as...Ch. 8.1 - WHAT IF? If you place a teaspoon of sugar in the...Ch. 8.2 - Cellular respiration uses glucose and oxygen,...Ch. 8.2 - VISUAL SKILLS How would the processes of...Ch. 8.2 - WHAT IF? Some nighttime partygoers wear glow-in-...Ch. 8.3 - How does ATP typically transfer energy from an...Ch. 8.3 - Prob. 2CCCh. 8.3 - MAKE CONNECTIONS Does Figure 8.11a show passive...Ch. 8.4 - Many spontaneous reactions occur very slowly. Why...
Ch. 8.4 - Prob. 2CCCh. 8.4 - WHAT IF? Malonate is an inhibitor of the enzyme...Ch. 8.4 - Prob. 4CCCh. 8.5 - How do an activator and an inhibitor have...Ch. 8.5 - Prob. 2CCCh. 8 - Explain how the highly ordered structure of a cell...Ch. 8 - Explain the meaning of each component in the...Ch. 8 - Describe the ATP cycle: How is ATP used and...Ch. 8 - How do both activation energy barriers and enzymes...Ch. 8 - Prob. 8.5CRCh. 8 - Choose the pair of terms that correctly completes...Ch. 8 - Prob. 2TYUCh. 8 - Which of the following metabolic processes can...Ch. 8 - Prob. 4TYUCh. 8 - Some bacteria art metabolically active in hot...Ch. 8 - If an enzyme is added to a solution where its...Ch. 8 - Prob. 7TYUCh. 8 - EVOLUTION CONNECTION Some people argue that...Ch. 8 - Prob. 9TYUCh. 8 - WRITE ABOUT A THEME: ENERGY AND MATTER Life...Ch. 8 - Prob. 11TYU
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Study Guide for Campbell Biology
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- 4. a. Calculate the KM (Michaelis constant) and the vmax (the maximum initial rate) for both substrates (sphingosine and ATP). Show your work, and be careful about units. b. threo-dihydrosphingosine, a stereoisomer of sphingosine, is an inhibitor of sphingosine kinase. What kind of inhibitor (competitive, uncompetitive, noncompetitive) is threo-dihydrosphingosine? Citing information from the Lineweaver-Burke plots, explain how you can tell.arrow_forward1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?arrow_forward1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in eachreaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 µM. a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? c. Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and KMfor the enzyme.arrow_forward
- 1. Provided in the Table below kinetic data for an enzymatic reaction that was carried out in the presence (last two columns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in eachreaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 µM. a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? c. Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and KM for the enzyme.arrow_forwardWHAT IF? Suppose the experiment had shown that class I mutants could grow only in MM supplementedby ornithine or arginine and that class II mutants could grow in MM supplemented by citrulline, ornithine,or arginine. What conclusions would the researchers have drawn from those results regarding the biochemicalpathway and the defect in class I and class II mutants?arrow_forward5. For a Michaelis-Menten enzyme, k1 = 5.2 ⅹ 108 M-1 s-1, k-1 = 3.1 ⅹ 104 s-1, and k2 = 3.4 ⅹ 105 s-1. a) Write out the reaction, showing k1, k-1, and k2. Calculate Ks and Km. Does substrate binding approach equilibrium or the steady state? Justify your answer. b) What is kcat for this reaction? Justify your answer. c) Calculate Vmax for the enzyme. The total enzyme concentration is 25 pmol L-1, and each enzyme has two active sites. d) What substrate concentration would be required for the reaction in (c) to reach half of Vmax. Justify your answer mathematically. e) A second Michaelis-Menten enzyme has k1 = 4.2 ⅹ 107 M-1 s-1, k-1 = 6.1 ⅹ 104 s-1, and k2 = 5.3 ⅹ 102 s-1. Which enzyme is most efficient? 6. A pharmaceutical company is trying to develop aarrow_forward
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- An enzyme catalyzes the reaction M↽−−⇀N M ↽ − − ⇀ N . The enzyme is present at a concentration of 2.0 nM 2.0 nM , and the ?max V max is 2.1 μM s−1 2.1 μM s − 1 . The ?m K m for substrate M M is 6.3 μM 6.3 μM . Calculate ?cat k cat .What values of ?max and ?m would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an α′ of 1.9?arrow_forwardCalculate α' for an inhibitor with KI' = 10.0 nmol L-1 when 100 nmol L-1 of inhibitor is present.arrow_forwardHello, For the image included: A) Which of the following statements are true of the malate dehydrogenase reaction in biochemical standard conditions? Choose all that apply. Group of answer choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium B) If the concentration of oxaloacetate is 107 times lower than the concentration of malate. Is the reaction spontaneous? Assume biochemical standard conditions. Group of answer choices No, because RTlnQ is very positive Yes, because RTlnQ is very positive No, because RTlnQ is very…arrow_forward
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