Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
10th Edition
ISBN: 9780133922851
Author: Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
Publisher: PEARSON
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Textbook Question
Chapter 9.3, Problem 3CC
VISUAL SKILLS Ø The conversions shown in Figure 9.10 and step 4 of Figure 9.12 are each catalyzed by a large multienzyme complex. What similarities are there in the reactions that occur in these two cases?
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Chemical scheme for enzyme catalysis (a) Write the chemical equations for enzyme,substrate, enzyme•substrate complex, and product as for a typical Michaelis-Mentenenzyme (b) At what condition is half of the enzyme expected to be saturated withsubstrate? (c) Plot the rate of product formation as a function of substrate concentration.(d) Indicate the KM parameter on your rate vs substrate plot.
Chapter 9 Solutions
Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
Ch. 9.1 - Prob. 1CCCh. 9.1 - WHAT IF? If the following redox reaction...Ch. 9.2 - VISUAL SKILLS During the redox reaction in...Ch. 9.3 - Prob. 1CCCh. 9.3 - What process in your cells produce the CO2 that...Ch. 9.3 - VISUAL SKILLS The conversions shown in Figure...Ch. 9.4 - WHAT IF? What effect would an absence of O2 have...Ch. 9.4 - WHAT IF? In the absence of O2 as in question 1,...Ch. 9.4 - MAKE CONNECTIONS Membranes must be fluid to...Ch. 9.5 - Consider the NADH formed during glycolysis. What...
Ch. 9.5 - WHAT IF? A glucose-fed yeast cell is moved from...Ch. 9.6 - MAKE CONNECTIONS Compare the structure of a fat...Ch. 9.6 - Prob. 2CCCh. 9.6 - Prob. 3CCCh. 9.6 - VISUAL SKILLS During intense exercise, can a...Ch. 9 - Describe the difference between the two processes...Ch. 9 - Which reactions in glycolysis are the source of...Ch. 9 - What molecular products indicate the complete...Ch. 9 - Briefly explain the mechanism by which ATP...Ch. 9 - Prob. 9.5CRCh. 9 - Prob. 9.6CRCh. 9 - Level 1: Knowledge/Comprehension 1. The immediate...Ch. 9 - Prob. 2TYUCh. 9 - 3. The final electron acceptor of the electron...Ch. 9 - Prob. 4TYUCh. 9 - What is the oxidizing agent in the following...Ch. 9 - When electrons flow along the electron transport...Ch. 9 - Prob. 7TYUCh. 9 - Prob. 8TYUCh. 9 - MAKE CONNECTIONS The proton pump shown in Figures...Ch. 9 - INTERPRET THE DATA Phosphofructokinase is an...Ch. 9 - DRAW IT The graph here shows the pH difference...Ch. 9 - EVOLUTION CONNECTION AIP synthases are found in...Ch. 9 - SCIENTIFIC INQUIRY In the 1930s, some physicians...Ch. 9 - WRITE ABOUT A THEME: ORGANIZATION In a short essay...Ch. 9 - SYNTHESIZE YOUR KNOWLEDGE Coenzyme Q (CoQ) is sold...
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- Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.arrow_forwardWhat is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1arrow_forwardGraph B above depicts Lineweaver-Burk double reciprocal plot for an enzyme catalyzed reaction carried out in the presence or absence of an inhibitor. Which of the following statement best describes the kinetic data shown below: ? Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 1 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a competitive inhibitor. Line 2 depicts the enzyme-catalyzed reaction carried out in the presence of a noncompetitive inhibitor.arrow_forward
- Hand written solutions are strictly prohibited.arrow_forwardPls help ASAP, thank you!arrow_forwardIf a reaction has a ΔG°′ value of at least −30.5 kJ · mol−1, suffi -cient to drive the synthesis of ATP (ΔG°′ = 30.5 kJ · mol−1), can it still drive the synthesis of ATP in vivo when its ΔG is only −10 kJ · mol−1? Explain.arrow_forward
- Kinetic Parameters of Enzyme-Catalyzed Reactions TABLE 12-1 The Values of KM, Keat, and Keat/KM for Some Enzymes and Substrates Enzyme Substrate KM (M) 9.5 x 10-5 1.2 x 10-² 2.6 x 10-2 2.5 x 10-2 4.4 x 10-1 8.8 x 10-2 6.6 x 10-4 Acetylcholinesterase Carbonic anhydrase Catalase Chymotrypsin Fumarase Urease Acetylcholine CO₂ HCO₁ H₂O₂ N-Acetylglycine ethyl ester N-Acetylvaline ethyl ester N-Acetyltyrosine ethyl ester Fumarate Malate Urea 5.0 x 10-6 2.5 x 10-5 2.5 x 10-2 Keat (S-¹) 1.4 x 104 1.0 × 106 4.0 × 105 1.0 X 107 5.1 x 10-2 1.7 × 10-1 1.9 X 10² 8.0 x 10² 9.0 × 10² 1.0 X 104 Keat/KM (M¹s¹) 1.5 × 108 8.3 x 107 1.5 x 107 4.0 X 108 1.2 x 10-1 1.9 2.9 × 105 1.6 × 108 3.6 X 107 4.0 X 105 Which enzyme is the most catalytically efficient? Which substrate does chymotrypsin bind to most tightly (assume k_₁ >> K₂)? Is fumarate or malate a better substrate of fumarase? Is it possible to have a kcat/KM of greater than 1 x 10⁹ M-¹ s-¹? Why or why not?arrow_forwardShown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R' H₂N _N_CH. сно CH₂ CH₂ CH₂ NH d=19H₂ NH₂ O CH- H₂C HN O CHarrow_forwardCould you help me with part F to H of the mechanism?: Using curved arrows, show the mechanism of each step labeled with a blue letter. Draw out abbreviated structures of the coenzymes, so that you can effectively show all arrow pushing. You may abbreviate the coenzymes by putting R groups on the molecule, but do draw out the parts of the structure that are involved in the arrow pushing. Please note that some of the transformations will require you to show multiple structures to show all of the arrow pushing (particularly some of the coenzyme-mediated steps). You do not need to show specific amino acid residues that perform the catalysis. You can abbreviate acidic amino acid residues “Enz–B–H” and basic residues “B–Enz”.arrow_forward
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