Campbell Biology: Australian And New Zealand Edition
11th Edition
ISBN: 9781488613715
Author: Tool_encoder.encodeforhtml(${ctx_requestparams.author})
Publisher: Pearson Education Australia
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 8.5, Problem 2CC
Summary Introduction
To determine: Involvement of ATP in the feedback inhibition of a catabolic pathway.
Introduction: Feedback inhibition is a mechanism in multistep pathways that aids in ceasing the reaction when one of the substrates is over produced. The substrate that is being over produced bind to one of the enzymes of the reaction. This will in turn stop the whole cycle of reactions because each step is interdependent.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Select all that apply.
What is true about the conformational aspects of coupling?
O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change.
O The conformational states interconvert as a result of proton flux through the synthase.
There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T).
Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis.
The Fo portion of ATP synthase acts as a rotary motor.
Need help
Outline 4 different ways a linear pathway can be inhibited. Of the 4 described, which would be the most effective and which would be the fastest mode of inhibition?
sapling learning
(a) Identify the group in pyridoxal phosphate (PLP) that covalently binds enzyme and substrate.
Hint
A
B
_H
OH
Previous
CH3
(b) Aminotransferases (transaminases) must deaminate one amino acid and add an amino group to another
amino acid during transamination. How do the two processes differ?
Map
The second part of the reaction (adding an amino group) is the reverse of the first (deamination).
The second part of the reaction takes place at a separate amino acid residue in the active site.
The first reaction involves the formation of a Schiff base, whereas the second does not.
The coenzyme PLP must be activated by an external amino group before it can catalyze the
removal of the amino group from the first amino acid.
Give Up & View Solution Check Answer Next
Exit
Chapter 8 Solutions
Campbell Biology: Australian And New Zealand Edition
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
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Recall that phosphonacetyl L - aspartate (PALA) is a potent inhibitor of ATCase because it mimics the two physiological substrates. However, in the presence of substrates, low concentrations of this unreactive bisubstrate analog increase the reaction velocity. On the addition of PALA, the reaction rate increases until an average of three molecules of PALA are bound per molecule of enzyme. This maximal velocity is 17-fold greater than it is in the absence of PALA. The reaction rate then decreases to nearly zero on the addition of three more molecules of PALA per molecule of enzyme. Why do low concentrations of PALA activate ATCase?arrow_forwardHi, help please. Discuss each method of regulating phosphofructokinase below as indicated by the circle. Discuss 1.) The type of regulation occurring, 2.) What compound or condition performs the regulation, 3.) How/why it influences the enzyme activity.arrow_forward. Propose a chemical mechanism for the reaction catalyzed by the PLP-dependent glatamate 1-semialdehyde aminomutase.arrow_forward
- Reminder: Enzymology is foundational to biochemistry. You should review and be familiar with the enzymes unit from BICH410. Here is a sample question as review!! Which of the following characteristics is(are) accurate in describing a regulated enzyme? Select all that apply. a) always responds the environment by covalent modification by phosphorylation b) displays only negative cooperativity c) contains multiple subunits d)has a defined T state and R statearrow_forwardI. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4arrow_forward. Consider the enzymatic reaction scheme: Asparagine + H20 Aspartate + NH3: a) calculate the specific activity of the enzyme, if in 30 seconds as a result of a reaction involving 3 mg of the enzyme under optimal conditions (pH 8.0, 37 °C) 75 umol aspartate is obtained; b) describe the reasons for the decrease in enzyme activity after incubation for 6. 10 minutes at 70 °C (provide an appropriate graph).arrow_forward
- A. Enzyme Kinetics Two compounds were being investigated by Al Cohol, a student researcher in Biochemistry, for their inhibitory effect on xanthine oxidase (XO). The inhibition of this enzyme is critical in the treating gouty arthritis. He uses xanthine (Xan) as substrate. He investigated two inhibitors namely kaempferol (Kmp) and chlorogenic acid (Cha). The data that he was able to acquire is given in Table 1 below. 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 A. Construct the Lineweaver-Burke plot for each reaction system in one graph using MS Excel. Copy and paste your graph with complete regression analysis.arrow_forwardPuting a metabolic pathway map together which includes glycolysis, gluconeogenesis, glycogen synthesis & glycogenolysis, and the two types of fermentation, and pyruvate oxidation (to acetyl-CoA). The map should have/illustrate/show all of the indicated 6 pathways stated previously on the same page, to emphasize how these processes are related to each other.  map should include:  a) Clear labels for all the pathways  b) All the pathways shown on the same page and correctly integrated with each other, i.e., it should be clear which reactions are shared by different pathways  c) The names of all metabolites (common abbreviations may be used)  d) The names of all enzymes  e) All relevant cofactors/co-substrates discussed in class, clearly showing, where ATP is used and produced  f) Double or single arrows representing reversible or irreversible reactions, respectively  g) All "high-energy" intermediates clearly labeled with an asterisk (*)  h) Labels for cellular locations of…arrow_forwardHelp is appreciated. Think of an unusual eukaryotic species in which its ATP synthase has 12 subunits for its c ring. How many ATP molecules can be produced per pair of electrons that traverse the respiratory chian starting at Complex I?  A. 2 ATP/2e- B. 1 ATP/2e- C. 0.5 ATP/2e- D. 1.5 ATP/2e- E. 3 ATP/2e-arrow_forward
- Fill in the blanks.: Write Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct, M if both statements are incorrect. A. An enzyme catalyzes a reaction by providing an alternative reaction pathway that has a lower energy of activation. B. The enthalpy of the enzyme-catalyzed reaction decreases significantly as compared to the uncatalyzed reaction.arrow_forward.Intramitochondrial ATP concentrations are about 5 mM, and phosphate con- centration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]arrow_forwardprotease mechanism: you isolate a new protease which cleaves the peptide bond 2 aa residues before a F residue. You might expect to fınd... O An I residue in the S2'pocket AL residue in the S2 pocket O aV residue in the oxyanion hole An Lresidue in the catalytic triad in Michaelis-Menton kinetics, cutting the enzyme concentration in half will O will double the reaction rate O will not change Vo and Vmax will change Vo but not turnover number decrease Km by halfarrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Anaerobic Respiration; Author: Bozeman Science;https://www.youtube.com/watch?v=cDC29iBxb3w;License: Standard YouTube License, CC-BY