EBK CAMPBELL BIOLOGY IN FOCUS
2nd Edition
ISBN: 8220101459299
Author: Reece
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.
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)
Chapter 6 Solutions
EBK CAMPBELL BIOLOGY IN FOCUS
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. 6.5 - How do an activator and an inhibitor have...Ch. 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 - SCIENTIFIC INQUIRY DRAW IT A researcher has...Ch. 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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- 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
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