EBK CAMPBELL BIOLOGY
10th Edition
ISBN: 9780136539414
Author: Reece
Publisher: VST
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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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Please explain each part thoroughly with explanations and answers given. This is Bipchemistry
Kk149.
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
EBK CAMPBELL BIOLOGY
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_forwardApproximately how much does staphylococcal nuclease (Table) decrease the activation free energy ΔG‡ of its reaction (the hydrolysis of a phosphodiester bond) at 25°C?arrow_forward
- Graph 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_forward2Larrow_forwardsub= 18 helparrow_forward
- Describe the mechanism of a-chymotrypsin. Explain the roles of constituents of the catalytic triad, their modes of catalysis, and the significance of the oxyanion hole in the catalysis.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_forwardKinetic 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_forward
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