CAMPBELL'S BIOLOGY MASTERING BIOLOGY
12th Edition
ISBN: 9780135855843
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
Biochemical 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 here
Please solve question correctly.
Hand written solutions are strictly prohibited.
Chapter 9 Solutions
CAMPBELL'S BIOLOGY MASTERING BIOLOGY
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
- sub= 18 helparrow_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
- Could you help me with a scheme following: Carboxylic acids do not readily undergo certain biochemical reactions; thus, they are often converted to thioesters or phosphonoesters for catalysis. What are two reactions that thioesters and phosphonoesters can undergo that carboxylic acids cannot? Show enzyme-catalyzed arrow pushing for both of these mechanisms.arrow_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_forwardChemical 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.arrow_forward
- Please help with all three parts of questionarrow_forwardMATHEMATICAL The free-energy change (G) for the oxidation of the cytochrome aa3 complex by molecular oxygen is 2102.3kJ=224.5kcal for each mole of electron pairs transferred. What is the maximum number of moles of ATP that could be produced in the process? How many moles of ATP are actually produced? What is the efficiency of the process, expressed as a percentage?arrow_forwardMake an electron-flow-mechanism for this synthetic scheme. This involves predicting major and by-products using electronic and structural effects. The arrow push mechanism must be shown.(from the reaction of α-ketoacids and oxaprolines to proteins that contain native serine residues ) with labelarrow_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