Biochemistry
9th Edition
ISBN: 9781305961135
Author: Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher: Cengage Learning
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Chapter 6, Problem 3RE
MATHEMATICAL Catalase breaks down hydrogen peroxide about
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61. MATHEMATICAL For the following aspartase reaction (see Ques-
tion 28) in the presence of the inhibitor hydroxymethylaspar-
tate, determine K and whether the inhibition is competitive or
noncompetitive.
[S]
(molarity)
V, No Inhibitor
(arbitrary units)
V, Inhibitor Present
(same arbitrary units)
:21×10¹01 0.026 TOIV 0.0109 9
5 X 10
0.092
0.040
0.086
0.120
10-3
IPO?
2.5 10-³
5×10 211 0.150 09M
ein
5 X 10-3
0.165
20 mys
0.142
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.
Calculate the Vmax of the reaction represented by Line (C). Show all mathematical work, please.
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.
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)…
Chapter 6 Solutions
Biochemistry
Ch. 6 - RECALL How does the catalytic effectiveness of...Ch. 6 - RECALL Are all enzymes proteins?Ch. 6 - MATHEMATICAL Catalase breaks down hydrogen...Ch. 6 - REFLECT AND APPLY Give two reasons why enzyme...Ch. 6 - RECALL For the reaction of glucose with oxygen to...Ch. 6 - REFLECT AND APPLY Would nature rely on the same...Ch. 6 - REFLECT AND APPLY Suggest a reason why heating a...Ch. 6 - REFLECT AND APPLY A model is proposed to explain...Ch. 6 - REFLECT AND APPLY Does the presence of a catalyst...Ch. 6 - REFLECT AND APPLY What effect does a catalyst have...
Ch. 6 - REFLECT AND APPLY An enzyme catalyzes the...Ch. 6 - REFLECT AND APPLY Can the presence of a catalyst...Ch. 6 - RECALL For the hypothetical reaction 3A+2B2C+3D...Ch. 6 - REFLECT AND APPLY The enzyme lactate dehydrogenase...Ch. 6 - REFLECT AND APPLY Would you use a pH meter to...Ch. 6 - REFLECT AND APPLY Suggest a reason for carrying...Ch. 6 - RECALL Distinguish between the lock-and-key and...Ch. 6 - RECALL Using an energy diagram, show why the...Ch. 6 - REFLECT AND APPLY Other things being equal, what...Ch. 6 - REFLECT AND APPLY Amino acids that are far apart...Ch. 6 - REFLECT AND APPLY If only a few of the amino acid...Ch. 6 - RECALL Show graphically how the reaction velocity...Ch. 6 - RECALL Define steady state, and comment on the...Ch. 6 - RECALL How is the turnover number of an enzyme...Ch. 6 - MATHEMATICAL For an enzyme that displays...Ch. 6 - MATHEMATICAL Determine the values of KM and Vmax...Ch. 6 - MATHEMATICAL The kinetic data in the following...Ch. 6 - MATHEMATICAL The enzyme -methylaspartase catalyzes...Ch. 6 - MATHEMATICAL The hydrolysis of a...Ch. 6 - MATHEMATICAL For the Vmax obtained in Question 26,...Ch. 6 - MATHEMATICAL You do an enzyme kinetic experiment...Ch. 6 - REFLECT AND APPLY The enzyme D-amino acid oxidase...Ch. 6 - REFLECT AND APPLY Why is it useful to plot rate...Ch. 6 - REFLECT AND APPLY Under what conditions can we...Ch. 6 - BIOCHEMICAL CONNECTIONS Why does acetazolamide...Ch. 6 - BIOCHEMICAL CONNECTIONS How did scientists...Ch. 6 - BIOCHEMICAL CONNECTIONS How do the KM values for...Ch. 6 - Prob. 38RECh. 6 - RECALL What are the three most common mechanisms...Ch. 6 - RECALL What is the biggest difference between a...Ch. 6 - RECALL How do scientists determine the KM of a...Ch. 6 - Prob. 42RECh. 6 - Prob. 43RECh. 6 - RECALL Do all enzymes display kinetics that obey...Ch. 6 - RECALL How can you recognize an enzyme that does...Ch. 6 - RECALL If we describe an enzyme like aspartate...Ch. 6 - RECALL How can competitive and pure noncompetitive...Ch. 6 - RECALL Why does a competitive inhibitor not change...Ch. 6 - RECALL Why does a pure noncompetitive inhibitor...Ch. 6 - RECALL Distinguish between the molecular...Ch. 6 - RECALL Can enzyme inhibition be reversed in all...Ch. 6 - RECALL Why is a Lineweaver-Burk plot useful in...Ch. 6 - RECALL Where do lines intersect on a...Ch. 6 - RECALL What is the difference between pure and...Ch. 6 - REFLECT AND APPLY Why can we say that having a...Ch. 6 - REFLECT AND APPLY When we compare the binding of I...Ch. 6 - RECALL Why does the apparent KM decrease in the...Ch. 6 - RECALL What is a suicide substrate? Why are they...Ch. 6 - RECALL If we made a Lineweaver-Burk plot of an...Ch. 6 - Prob. 60RECh. 6 - MATHEMATICAL For the following aspartase reaction...Ch. 6 - REFLECT AND APPLY Is it good (or bad) that enzymes...Ch. 6 - REFLECT AND APPLY Noncompetitive inhibition is a...Ch. 6 - BIOCHEMICAL CONNECTIONS You have been hired by a...Ch. 6 - REFLECT AND APPLY Would you expect an irreversible...Ch. 6 - REFLECT AND APPLY Would you expect the structure...Ch. 6 - Prob. 67RECh. 6 - Prob. 68RE
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- MATHEMATICAL Using the information in Table 20.2, calculate G for the following reaction: 2Cytaa3[oxidized;Fe(III)]+2Cytb[reduced;Fe(II)]2Cytaa3[reduced;Fe(II)]+2Cytb[oxidized;Fe(III)]arrow_forwardMATHEMATICAL For an enzyme that displays MichaelisMenten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? (a) [S]=KM (b) [S]=0.5KM (c) [S]=0.1KM (d) [S]=2KM (e) [S]=10KMarrow_forwardMATHEMATICAL For the Vmax obtained in Question 26, calculate the turnover number (catalytic rate constant) assuming that 131024mol of enzyme were used.arrow_forward
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