CAMPBELL BIOLOGY IN FOCUS (LL)-W/MOD.MA
3rd Edition
ISBN: 9780135686065
Author: Urry
Publisher: PEARSON
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Textbook Question
Chapter 6.4, Problem 3CC
WHAT IF? Malonate is an inhibitor of the enzyme succinate dehydrogenase. How would you determine whether malonate is a competitive or noncompetitive inhibitor?
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WHAT IF? Regulation of isoleucine synthesis is anexample of feedback inhibition of an anabolic pathway.With that in mind, explain how ATP might be involvedin feedback inhibition of a catabolic pathway.
. The steady-state kinetics of an enzyme are studied in the absence and pres-
ence of an inhibitor (inhibitor A). The initial rate is given as a function of
substrate concentration in the following table:
v[(mmol/L)min ']
[S] (mmol/L.)
No inhibitor
Inhibitor A
1.25
1.72
0.98
1.67
2.04
1.17
2.50
2.63
1.47
5.00
3.33
1.96
10.00
4.17
2.38
(a) What kind of inhibition (competitive, uncompetitive, or mixed) is
involved?
(b) Determine Vmax and KM in the absence and presence of inhibitor.
Thank you in advance!Based on the model on the picture, please help me identify these (even with no explanation):
4 What are the factors that affect △G?
5. What is energy coupling? In a coupling reaction, what must be the overall value of △G?
6. What does the cell do with the energy produced from exergonic reactions?
7. What molecule does the cell use as an energy carrier? Draw its structure.
8. Why is it that this energy carrier is considered to be high energy containing phosphate?
9. Bond of this energy carrier of cells is broken through what?
Chapter 6 Solutions
CAMPBELL BIOLOGY IN FOCUS (LL)-W/MOD.MA
Ch. 6.1 - MAKE CONNECTIONS How does the second law of...Ch. 6.1 - Describe the forms of energy found in an apple as...Ch. 6.2 - Cellular respiration uses glucose and oxygen,...Ch. 6.2 - Prob. 2CCCh. 6.2 - Prob. 3CCCh. 6.3 - How does ATP typically transfer energy from...Ch. 6.3 - Prob. 2CCCh. 6.3 - MAKE CONNECTIONS Does Figure 6.10a show passive or...Ch. 6.4 - Many spontaneous reactions occur very slowly. Why...Ch. 6.4 - Why do enzymes act only on very specific...
Ch. 6.4 - WHAT IF? Malonate is an inhibitor of the enzyme...Ch. 6.4 - A mature lysosome has an internal pH of around...Ch. 6.5 - How do an activator and an inhibitor have...Ch. 6.5 - Prob. 2CCCh. 6 - Choose the pair of terms that correctly completes...Ch. 6 - Prob. 2TYUCh. 6 - Which of the following metabolic processes can...Ch. 6 - If an enzyme in solution is saturated with...Ch. 6 - Some bacteria are metabolically active in hot...Ch. 6 - If an enzyme is added to a solution where its...Ch. 6 - DRAW IT Using a series of arrows, draw the...Ch. 6 - Prob. 8TYUCh. 6 - SCIENCE, TECHNOLOGY, AND SOCIETY Organophosphates...Ch. 6 - FOCUS ON EVOLUTION A recent revival of the...Ch. 6 - FOCUS ON ENERGY AND MATTER Life requires energy....Ch. 6 - SYNTHESIZE YOUR KNOWLEDGE Explain what is...
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- Inhibitor X exerts which of the following effects on the above enzyme (maltase)? (inhibitor X changes maltase activity to a V o of 0.10 mM per minute when [S] = 0.125 mM, and a V o of 0.25 mM per minute when [S] = 0.50 mM)arrow_forwardSelect 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.arrow_forwardEnzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?arrow_forward
- Help please. This question is specifically asking for the identification of the biomolecules that are attached to the sphingosine core, then we need to answer what bond causes those biomolecules to be connected to the sphingosine, what reaction created that bond (maybe addition or oxidation etc.), what were the starting materials and lastly what reagents or conditions are needed for the reaction to occur. Thank you!arrow_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_forwardLet’s consider vmax. Recall that uncompetitive inhibitors bind to the enzyme only after thesubstate is bound.a) As the concentration of substrate increases, the fraction of enzyme bound to substrate (circleone) increases / decreases?b) Does an uncompetitive inhibitor bind more readily when the substrate concentration is low orhigh?arrow_forward
- What 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_forwardSuppose that the data below are obtained for an enzyme catalyzed reaction in the presence and absence of inhibitor Y. [S] (mM) V (mmol/mL*min) Without Y With Y 0.2 5.0 2.0 0.4 7.5 3.0 1.8 10.0 4.0 1.0 10.7 4.3 2.0 12.5 5.0 4.0 13.6 5.5 a.) Determine the type of inhibition that has occurred b.) Does inhibitor Y combine with E, with ES or with both? Explain c.) Calculate the inhibitor constant, Ki, for substance Y, assuming that the final concentration of Y in the reaction mixture was 0.3mMarrow_forwardReaction rate 0.35 0.30 0.25 0.20 0.15- 0.10 0.05 0.00 0 1000 2000 Enzyme total is 5mM 3000 4000 1. Substrate concentration 1. The above graph is an enzyme reaction, what is the vMax, KM, and Kcat of this enzymatic reaction? What does vMax, kM and Kcat mean, explain? 2. What are the three forms of regulation that follow the Michaelis Menten kinetics? What are the mechanisms by which these inhibitors can regulate the enzyme?arrow_forward
- 5. By using Excel or GoogleSheets. graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Kwax values for the inhibited and uninhibited reactions? Is the inhibitor competitive or noncompetitive? [S] (mM) V, No Inhibitor (mmol min-) V, Inhibitor Present (mmol min-') 1 × 10-4 5 × 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 0.026 0.010 0.092 0.136 0.040 0.086 0.150 0.120 0.165 0.142arrow_forwardFill 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_forwardsapling 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 Exitarrow_forward
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