CAMPBELL BIOLOGY MOD MASTERING (18 WEEK)
12th Edition
ISBN: 9780136920335
Author: Urry
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Question
Chapter 9.3, Problem 3CC
Summary Introduction
To compare: The multi-enzyme complex involved in the conversion of pyruvate to acetyl CoA with the multienzyme complex that catalyzes Step 4 of the Citric acid cycle.
Introduction:
The citric acid cycle is a cyclic
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Hello! By what process can I arrive at the answer? Please be detailed on the problem should be done, thanks!
pls help
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?
Chapter 9 Solutions
CAMPBELL BIOLOGY MOD MASTERING (18 WEEK)
Ch. 9.1 - Compare and contrast aerobic and anaerobic...Ch. 9.1 - WHAT IF? If the following redox reaction...Ch. 9.2 - Prob. 1CCCh. 9.3 - Prob. 1CCCh. 9.3 - What process in your cells produce the CO2 that...Ch. 9.3 - Prob. 3CCCh. 9.4 - Prob. 1CCCh. 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 - Prob. 4CCCh. 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 - Prob. 3TYUCh. 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 - Prob. 9TYUCh. 9 - Prob. 10TYUCh. 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...
Knowledge Booster
Similar questions
- Pls help due asaparrow_forwardBiochemical Reactions Using good details, compare and contrast the pairs of different biochemical reactions. Create your own comparing and contrasting map similar to the one below to show your understanding. Anabolism Catabolism First Pair of Describe Describe differences here différences here Reaction Types Describe similarities here Second Describe Pair of differences here Reaction Types Describe similarties here Describe differences here Pair of Reaction Describe sampar lus heru Types Describe Par of 110 Describe differences here Describe différences here Describe differences herearrow_forwardPlease solve question correctly.arrow_forward
- Please explain parts D and E only. Reposting for continued responses. This is Biochem. Please explain each part thoroughly.arrow_forwardBased on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the Vmax of the reaction represented by Line (C). Show all mathematical work, please.arrow_forwardBased on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Which of the following statements is true? Select any/all answers that apply. A. Both types of inhibitor mediate a slope effect on the Lineweaver-Burke plot. B. Both types of inhibitor decrease the apparent Vmax for this enzyme-catalyzed reaction. C. Both types of inhibitor alter the apparent Km of this enzyme-catalyzed reaction. D. Lines (A) and (C) share the same X-intercept, indicating that the noncompetitive inhibitor decreases the apparent Km of this enzyme-catalyzed reaction. E. Lines (A) and (C)…arrow_forward
- Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. QUESTION: Line (A) represents ____________. A. an enzyme-catalyzed reaction in the absence of any inhibitor. B. an enzyme-catalyzed reaction in the presence of a competitive inhibitor. C. an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor. D. an enzyme-catalyzed reaction in the presence of a noncompetitive, or mixed, inhibitor.arrow_forwardBased on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the Km of the reaction represented by Line (B).arrow_forwardENZYME KINETICS ANALYSIS of 6 Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess causes gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student researcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO which uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the Lineweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table 2 and paste a copy of your Lineweaver-Burk plot. submit the picture of your output in PNG or JPG format. Table 1. Enzyme Kinetic Data Velocity, mM/s [S], mM Хan Kmp Cha 0.492 0.0678 0.0351 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Table 2. Enzyme Kinetic Parameters Xanthine Kaempferol Chlorogenic acid Parameters Vmax Км Type of Inhibition Mode of Binding NA NA Lineweaver-Burk Plotarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning