Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th Edition)
10th Edition
ISBN: 9780133922851
Author: Jane B. Reece, Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Robert B. Jackson
Publisher: PEARSON
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Chapter 8, Problem 4TYU
Summary Introduction
Introduction: Enzymes are macromolecules, which acts like the catalysts that increases the reaction without itself undergoing any change or without being consumed. Enzymes are the proteins.
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A mixed inhibitor of an enzyme (sometimes called a mixed non-competitive inhibitor) can decrease the rate of a reaction by any of the following EXCEPT by:
a) binding to a site other than the active site of the enzyme.
b) binding to the active site of the enzyme, preventing substrate binding.
c) decreasing kcat.
d) Increasing KM.
A competitive inhibitor diminishes the rate of catalysis:
A) By reducing the proportion of enzyme molecules bound to a substrate.
OB) By altering the shape of the active site of the enzyme
C) By binding to a regulatory subunit
D) By enhancing the interaction between enzyme and reaction product
Vmax for an enzyme-catalyzed reaction:
A)
generally increases when pH increases.
B)
is limited only by the amount of substrate supplied.
C)
is twice the rate observed when the concentration of substrate is equal to the Km.
D)
is unchanged in the presence of a uncompetitive inhibitor.
E)
increases in the presence of a competitive inhibitor.
Chapter 8 Solutions
Campbell Biology, Books a la Carte Plus Mastering Biology with eText -- Access Card Package (10th 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
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- Vmax for an enzyme-catalyzed reaction: A)is twice the rate observed when the concentration of substrate is equal to Km. B)is unchanged in the presence of a noncompetitive inhibitor. C)generally increases when pH increases. D)increases in the presence of a competitive inhibitor. E)is limited only by the amount of substrate supplied.arrow_forwardEnzyme specificity us given by :- а) Km b) Vmax c) both d) nonearrow_forwarda) How do enzymes catalyze (increase the rate of) reactions? b) What does it mean that enzymes are “substrate specific”? c) How are they usually namearrow_forward
- Based on the kinetic constants below, which enzyme will most efficiently catalyze conversion of the substrate into product? A) Vmax = 10 uM s-1, KM = 10 µM B) Vmax = 10 uM s-1, KM = 0.01 µM C) Vmax = 1000 uM s-1, KM = 500 µM D) Vmax = 1 uM s-1, KM = 1 µM E) Vmax = 200 uM s-1, KM = 10 µMarrow_forwardMULTIPLE CHOICE Compared to an uncatalyzed reaction, an enzyme-catalyzed reaction ________. A) uses less substrate B) produces different products C) occurs at a faster rate D) requires more energy E) requires a higher temperaturearrow_forwardAll of the following statements about competitive and non-competitive inhibitors are true EXCEPT:(a) Competitive inhibitors are structurally similar to anenzyme’s substrate and bind to the enzyme’s allostericsite.(b) Competitive inhibitors work by competing with a sub-strate for binding to an enzyme’s active site.(c) Noncompetitive inhibitors can bind at sites other thanthe active site of an enzyme, distorting the tertiary pro-tein structure, which alters the shape of the active site,rendering it ineffective for substrate binding.(d) Some noncompetitive inhibitors bind reversibly whilesome bind irreversibly to their enzyme.(e) b and d.arrow_forward
- the type of enzyme inhibition in which covalent bulky adduct prevents catalysis is ? a) uncompetitive b) reversible c) noncompetitive d) competitive e) Irreversiblearrow_forwardWhich model for enzyme-substrate chemical complementarity is described by the following: Before substrate binding, some enzyme molecules have active sites complementary to substrates and other enzyme molecules have non-complementary active sites. Substrate molecules preferentially bind to the enzyme molecules with complementary active sites. Non-complementary enzyme molecules undergo a structural change to become complementary to maintain conformational equilibrium. a) conformational selection b) induced fit c) lock and key...arrow_forwardWhich of the following is true under the following conditions: an enzyme displaying Michaelis-Menten kinetics where the enzyme concentration is 10 nM, the substrate concentration is 45 mM, and the Km is 50 µM? a) The enzyme has low catalytic efficiency for the substrate. b)The rate of catalysis is near half-maximal velocity. c)The enzymatic reaction is near maximal velocity. d)Halving the substrate concentration has little effect on the catalytic rate. e) There is not enough information provided.arrow_forward
- Choose the best answer The active site of an enzyme is the place where the following happens: a)The enzyme-substrate complex forms and the reaction occurs at the active site. b)The enzyme substrate complex forms here. c)The catalytic reaction happens here. d)Allosteric regulation of enzyme rate occurs here. e)All of these are correct.arrow_forwardA biochemist discovers and purifies a new enzyme, generating the purification table below. (a) From the information given in the table, calculate the specific activity of the enzyme after each purification procedure.(b) Which of the purification procedures used for this enzyme is most effective (i.e., gives the greatest relative increase in purity)?(c) Which of the purification procedures is least effective?(d) Is there any indication based on the results shown in the table that the enzyme after step 6 is now pure? What else could be done to estimate the purity of the enzyme preparation?arrow_forwardWhich enzyme would have the greatest catalytic efficiency? a) Km 20 nM; kcat 50 s-1 b) Km 0.04 uM; kcat 50 s-1 c) Km 10 nM; kcat 5 s-1 d) Km 40 nM; kcat 25 s-1arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License