Chemical Principles: The Quest for Insight
7th Edition
ISBN: 9781464183959
Author: Peter Atkins, Loretta Jones, Leroy Laverman
Publisher: W. H. Freeman
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 7, Problem 7E.9E
Interpretation Introduction
Interpretation:
Michaelis-Menten rate equation has to be derived. The graph of
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction.
Vmax [S]
U =
Km + [S]
where v is the velocity, or rate, Vmax is the maximum velocity, Km is the Michaelis-Menten constant, and [S] is the
substrate concentration.
A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (vo) at different substrate concentrations
([S]).
First, move the line labeled Vmax to a position that represents
the maximum velocity of the enzyme.
300
V
Next, move the line labeled 1/2 Vmax to its correct position.
max
275
Then, move the line labeled Km to its correct position.
250
225
200
175
Michaelis–Menten curve
150
K
a 125
m
100
1/2 V
75
max
50
25
10
20
30
40
50
60
70
80
90
100
[S] (µM)
Incorrect
Estimate the values for Vmax and Km.
Vmax
175
µM/min
Km
14
µM
v (µM/min)
Our body obtains energy from the combustion of glucose. During this process, glycerate is transformed first into pyruvate. This
reaction has an activation energy close to 44 kJ. Estimate how many times faster this reaction is when someone has a high fever
close to 106 F (41 oC) compared to its rate at normal body temperature (98.6 F; 37 oC).
Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer.
a
b
с
d
31% faster
11% faster
24% faster
259% faster
Your answer
A reaction has Keq' = 120. The rate constant of this reaction was found
to be 1.11x 101s-1.
If the catalytic power of an enzyme for this reaction is 1.25 x 10', what
is the rate constant, in s1, for the reverse direction of the catalyzed
reaction?
Chapter 7 Solutions
Chemical Principles: The Quest for Insight
Ch. 7 - Prob. 7A.1ASTCh. 7 - Prob. 7A.1BSTCh. 7 - Prob. 7A.2ASTCh. 7 - Prob. 7A.2BSTCh. 7 - Prob. 7A.3ASTCh. 7 - Prob. 7A.3BSTCh. 7 - Prob. 7A.4ASTCh. 7 - Prob. 7A.4BSTCh. 7 - Prob. 7A.1ECh. 7 - Prob. 7A.2E
Ch. 7 - Prob. 7A.3ECh. 7 - Prob. 7A.4ECh. 7 - Prob. 7A.7ECh. 7 - Prob. 7A.8ECh. 7 - Prob. 7A.9ECh. 7 - Prob. 7A.10ECh. 7 - Prob. 7A.11ECh. 7 - Prob. 7A.12ECh. 7 - Prob. 7A.13ECh. 7 - Prob. 7A.14ECh. 7 - Prob. 7A.15ECh. 7 - Prob. 7A.16ECh. 7 - Prob. 7A.17ECh. 7 - Prob. 7A.18ECh. 7 - Prob. 7B.1ASTCh. 7 - Prob. 7B.1BSTCh. 7 - Prob. 7B.2ASTCh. 7 - Prob. 7B.2BSTCh. 7 - Prob. 7B.3ASTCh. 7 - Prob. 7B.3BSTCh. 7 - Prob. 7B.4ASTCh. 7 - Prob. 7B.4BSTCh. 7 - Prob. 7B.5ASTCh. 7 - Prob. 7B.5BSTCh. 7 - Prob. 7B.1ECh. 7 - Prob. 7B.2ECh. 7 - Prob. 7B.3ECh. 7 - Prob. 7B.4ECh. 7 - Prob. 7B.5ECh. 7 - Prob. 7B.6ECh. 7 - Prob. 7B.7ECh. 7 - Prob. 7B.8ECh. 7 - Prob. 7B.9ECh. 7 - Prob. 7B.10ECh. 7 - Prob. 7B.13ECh. 7 - Prob. 7B.14ECh. 7 - Prob. 7B.15ECh. 7 - Prob. 7B.16ECh. 7 - Prob. 7B.17ECh. 7 - Prob. 7B.18ECh. 7 - Prob. 7B.19ECh. 7 - Prob. 7B.20ECh. 7 - Prob. 7B.21ECh. 7 - Prob. 7B.22ECh. 7 - Prob. 7C.1ASTCh. 7 - Prob. 7C.1BSTCh. 7 - Prob. 7C.2ASTCh. 7 - Prob. 7C.2BSTCh. 7 - Prob. 7C.1ECh. 7 - Prob. 7C.2ECh. 7 - Prob. 7C.3ECh. 7 - Prob. 7C.4ECh. 7 - Prob. 7C.5ECh. 7 - Prob. 7C.6ECh. 7 - Prob. 7C.7ECh. 7 - Prob. 7C.8ECh. 7 - Prob. 7C.9ECh. 7 - Prob. 7C.11ECh. 7 - Prob. 7C.12ECh. 7 - Prob. 7D.1ASTCh. 7 - Prob. 7D.1BSTCh. 7 - Prob. 7D.2ASTCh. 7 - Prob. 7D.2BSTCh. 7 - Prob. 7D.1ECh. 7 - Prob. 7D.2ECh. 7 - Prob. 7D.3ECh. 7 - Prob. 7D.5ECh. 7 - Prob. 7D.6ECh. 7 - Prob. 7D.7ECh. 7 - Prob. 7D.8ECh. 7 - Prob. 7E.1ASTCh. 7 - Prob. 7E.1BSTCh. 7 - Prob. 7E.1ECh. 7 - Prob. 7E.2ECh. 7 - Prob. 7E.3ECh. 7 - Prob. 7E.4ECh. 7 - Prob. 7E.5ECh. 7 - Prob. 7E.6ECh. 7 - Prob. 7E.7ECh. 7 - Prob. 7E.8ECh. 7 - Prob. 7E.9ECh. 7 - Prob. 1OCECh. 7 - Prob. 7.1ECh. 7 - Prob. 7.2ECh. 7 - Prob. 7.3ECh. 7 - Prob. 7.4ECh. 7 - Prob. 7.5ECh. 7 - Prob. 7.6ECh. 7 - Prob. 7.7ECh. 7 - Prob. 7.9ECh. 7 - Prob. 7.11ECh. 7 - Prob. 7.14ECh. 7 - Prob. 7.15ECh. 7 - Prob. 7.17ECh. 7 - Prob. 7.19ECh. 7 - Prob. 7.20ECh. 7 - Prob. 7.23ECh. 7 - Prob. 7.25ECh. 7 - Prob. 7.26ECh. 7 - Prob. 7.29ECh. 7 - Prob. 7.30ECh. 7 - Prob. 7.31E
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.Similar questions
- List two ways that enzyme catalysis of a reaction is superior to normal conditions.arrow_forwardDescribe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.arrow_forwardCompare the lock-and-key and induced-fit models for substrate binding to an enzyme.arrow_forward
- When an enzyme is added to a solution (1.0 mL) containing its substrate at a concentration of 100 times the Km, it catalyzes the conversion of 75 mol of the substrate into the product in 3.0 min in the 1.0 mL solution. The concentration of enzyme in the solution is 0.20 M. What is the enzyme's turnover number (kcat)? Note that the unit of kcat is min-1.arrow_forwardThe Arrhenius equation quantifies which of the following effects? the pre-orientation effect in heterogeneous catalysts temperature increasing the percent of successful collisions substrate concentration in enzyme-catalyzed reactions O pressure increasing the overall number of collisions activation energy reduction in homogeneous catalystsarrow_forwardI want clear handwritten solution only.arrow_forward
- At pH = 7, the measured Michaelis constant and maximum velocity for the enzymatic conversion of fumarate to L-malate, Fumarate + H2O → L-Malate are 4.0 x 10-6 M and 1.3 x 10 3 [E]0 s-1 , respectively, where [E]0 is the total molar concentration of the enzyme. The Michaelis constant and maximum velocity for the reverse reaction are 1.0 x 10-5 M and 800 [E]0 s-1 , respectively. 8A)WHAT is the equilibrium constant (a value) for the hydration reaction? [Notes: the arrow above is an equilibrium arrow. The activity of water is set equal to unity] 8B.) DRAW all chemical entities in the forward, balanced chemical reaction, above.arrow_forwardthe Arrhenius equation reveals how temperature affects the rate constant k. (a) use what you know from the Arrhenius equation to make a rough plot of the rate (y-axis) vs. temperature (x-axis) of a simple chemical reaction. (b) explain why if you measured the rate of an enzyme catalyzed reaction at vary thing temperature and plotted the results, you would get a bell-shaped curve in which the rate increases with T up to a point, and then rapidly falls offarrow_forwardTime [Z] (hours) (mg/L) |160 2 |140 3 |130 6 100 8 80 10 |60 |12 40 Calculate k, the elimination rate constant, responsible for drug degradation (in mg/L*hr).arrow_forward
- Suppose that a certain biologically important reaction is quite slow at physiological temperature (37 °C) in the absence of a catalyst Part A Assuming that the collision factor remains the same, by how much must an enzyme lower the activation energy of the reaction in order to achieve a 5x105-fold increase in the reaction rate? Express your answer in kilojoules per mole to one significant figure. ΠΕΙ ΑΣΦ Ea,uncatalyzed - Ea,catalyzed 148 Sulmit Previous Answers Request Answer M Incorrect: Try Again: One attempt remaining Review Constants | Periodic Table ? kJ/molarrow_forwardThe chemical equation corresponding to the hydrolysis reaction can be written: R-CI + H,O →R-OH+ CI+H* Let's call a the initial concentration in 2-chloro-2-methyl-butane and x the concentration of hydrochloric acid that is formed at time t. Water remains in large excess all over the course of the reaction. Then one can write: R-CI+ H,0 –R-OH+ CI +H+ t = 0 a 0 0 0 t>0 t = 00 05: Recall the Arrhenius law and explain the meaning and unit of the individual terms. Deduce an expression of the activation energy as a function of two temperatures T1 and T2.arrow_forwardBe sure to answer all parts. In acidic solution, the breakdown of sucrose into glucose and fructose has this rate law: kH |sucrose ]. The initial rate of sucrose breakdown is measured in a solution that is 0.01 M H, 1.0 M sucrose, 0.1 M fructose, and 0.1 M glucose. How does the rate change if rate = (a) [Sucrose] is changed to 2.5 M? (select) (b) [Sucrose], [fructose], and Iglucose] are all changed to 0.5 M? (select) (c) H*] is changed to 0.001 M? (select) (d) [Sucrose] and H* are both changed to 0.1 M? (select)arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Chemistry: The Molecular ScienceChemistryISBN:9781285199047Author:John W. Moore, Conrad L. StanitskiPublisher:Cengage Learning
Chemistry & Chemical ReactivityChemistryISBN:9781337399074Author:John C. Kotz, Paul M. Treichel, John Townsend, David TreichelPublisher:Cengage Learning
Introductory Chemistry: An Active Learning Approa...ChemistryISBN:9781305079250Author:Mark S. Cracolice, Ed PetersPublisher:Cengage Learning
Chemistry for Engineering StudentsChemistryISBN:9781285199023Author:Lawrence S. Brown, Tom HolmePublisher:Cengage Learning
Chemistry for Today: General, Organic, and Bioche...ChemistryISBN:9781305960060Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. HansenPublisher:Cengage Learning
Chemistry & Chemical ReactivityChemistryISBN:9781133949640Author:John C. Kotz, Paul M. Treichel, John Townsend, David TreichelPublisher:Cengage Learning
Chemistry: The Molecular Science
Chemistry
ISBN:9781285199047
Author:John W. Moore, Conrad L. Stanitski
Publisher:Cengage Learning
Chemistry & Chemical Reactivity
Chemistry
ISBN:9781337399074
Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Publisher:Cengage Learning
Introductory Chemistry: An Active Learning Approa...
Chemistry
ISBN:9781305079250
Author:Mark S. Cracolice, Ed Peters
Publisher:Cengage Learning
Chemistry for Engineering Students
Chemistry
ISBN:9781285199023
Author:Lawrence S. Brown, Tom Holme
Publisher:Cengage Learning
Chemistry for Today: General, Organic, and Bioche...
Chemistry
ISBN:9781305960060
Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen
Publisher:Cengage Learning
Chemistry & Chemical Reactivity
Chemistry
ISBN:9781133949640
Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Publisher:Cengage Learning
Enzymes - Effect of cofactors on enzyme; Author: Tutorials Point (India) Ltd;https://www.youtube.com/watch?v=AkAbIwxyUs4;License: Standard YouTube License, CC-BY
Enzyme Catalysis Part-I; Author: NPTEL-NOC IITM;https://www.youtube.com/watch?v=aZE740JWZuQ;License: Standard Youtube License