EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
7th Edition
ISBN: 8220100853180
Author: STOKER
Publisher: CENGAGE L
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 21, Problem 21.28EP
Indicate whether each of the statements in Problem 21-26 applies to (1) the lock-and-key model for enzyme action, (2) the induced-fit model for enzyme action, (3) both models, or (4) neither model.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
If a michaelis-type enzyme has an apparent
Km of 2*10^-8 and apparent Vmax of
1*10^-4 moles/min in the presence of
1*10^-3 M uncompetitive inhibitor
(Ki=1*10^-7 M), what is the true Km of the
enzyme
What is the difference between the lock-and-key model of enzyme action and the induced-fit model?
The Lineweaver-Burke plot was originally developed in order to "linearize" the data
obtained from enzyme kinetics experiments, in order to facilitate the determination
of kinetic parameters. Why is it not considered to be an accurate method for this
purpose?
It is very difficult to draw a straight line on a computer.
It is very difficult to calculate the variables required for the "x" and "y" axis.
It is more accurate to use the standard "V versus [S]" plot to determine Vmax
and KM-
The plot weights the least accurate data points the most heavily.
It is no longer considered to be acceptable to extrapolate from known data.
Chapter 21 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
Ch. 21.1 - Which of the following statements concerning the...Ch. 21.1 - Prob. 2QQCh. 21.2 - Which of the following statements about a...Ch. 21.2 - Which of the following statements about cofactors...Ch. 21.2 - Prob. 3QQCh. 21.3 - Which of the following statements concerning an...Ch. 21.3 - Prob. 2QQCh. 21.3 - Which of the following pairings of enzyme type and...Ch. 21.3 - Which of the following pairings of enzyme type and...Ch. 21.4 - Prob. 1QQ
Ch. 21.4 - Which of the following statements concerning the...Ch. 21.4 - Prob. 3QQCh. 21.5 - The specificity of an enzyme that catalyzes the...Ch. 21.5 - Prob. 2QQCh. 21.6 - The number of substrate molecules converted to...Ch. 21.6 - Prob. 2QQCh. 21.6 - Prob. 3QQCh. 21.7 - Extremozyme presence is not possible in which of...Ch. 21.7 - Prob. 2QQCh. 21.8 - Prob. 1QQCh. 21.8 - Prob. 2QQCh. 21.8 - Prob. 3QQCh. 21.9 - Prob. 1QQCh. 21.9 - Prob. 2QQCh. 21.9 - Prob. 3QQCh. 21.10 - Prob. 1QQCh. 21.10 - Prob. 2QQCh. 21.11 - Prob. 1QQCh. 21.11 - Prob. 2QQCh. 21.12 - Prob. 1QQCh. 21.12 - Prob. 2QQCh. 21.12 - Prob. 3QQCh. 21.13 - Prob. 1QQCh. 21.13 - Prob. 2QQCh. 21.13 - In the recharging of a metal-containing enzyme by...Ch. 21.14 - Prob. 1QQCh. 21.14 - Prob. 2QQCh. 21.14 - Prob. 3QQCh. 21.14 - Which of the B vitamins has a name that draws...Ch. 21.14 - Prob. 5QQCh. 21.14 - Prob. 6QQCh. 21.15 - Prob. 1QQCh. 21.15 - Prob. 2QQCh. 21.15 - Prob. 3QQCh. 21.15 - For which of the following vitamins is blood...Ch. 21.15 - Prob. 5QQCh. 21 - What is the general role of enzymes in the human...Ch. 21 - Why does the body need so many different enzymes?Ch. 21 - Prob. 21.3EPCh. 21 - Prob. 21.4EPCh. 21 - Indicate whether each of the following phrases...Ch. 21 - Indicate whether each of the following phrases...Ch. 21 - Explain why a metal ion can function as a cofactor...Ch. 21 - Prob. 21.8EPCh. 21 - Prob. 21.9EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Prob. 21.11EPCh. 21 - Based on its name, indicate whether each of the...Ch. 21 - Predict the function of each of the following...Ch. 21 - Predict the function of each of the following...Ch. 21 - Prob. 21.15EPCh. 21 - Prob. 21.16EPCh. 21 - Prob. 21.17EPCh. 21 - Suggest a name for an enzyme that catalyzes each...Ch. 21 - Prob. 21.19EPCh. 21 - Prob. 21.20EPCh. 21 - To which of the six major classes of enzymes does...Ch. 21 - To which of the six major classes of enzymes does...Ch. 21 - Identify the enzyme needed in each of the...Ch. 21 - Identify the enzyme needed in each of the...Ch. 21 - Prob. 21.25EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Indicate whether each of the statements in Problem...Ch. 21 - Indicate whether each of the statements in Problem...Ch. 21 - Prob. 21.29EPCh. 21 - Prob. 21.30EPCh. 21 - Prob. 21.31EPCh. 21 - Prob. 21.32EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Indicate whether each of the following statements...Ch. 21 - Prob. 21.35EPCh. 21 - Prob. 21.36EPCh. 21 - Prob. 21.37EPCh. 21 - Prob. 21.38EPCh. 21 - What type of specificity (absolute, group,...Ch. 21 - What type of specificity (absolute, group,...Ch. 21 - The following graph shows the relationship between...Ch. 21 - Based on the graphical information in Problem...Ch. 21 - Prob. 21.43EPCh. 21 - Based on the graphical information in Problem...Ch. 21 - Prob. 21.45EPCh. 21 - Prob. 21.46EPCh. 21 - Draw a graph that shows the effect of increasing...Ch. 21 - Prob. 21.48EPCh. 21 - Prob. 21.49EPCh. 21 - What is an enzyme turnover number?Ch. 21 - Describe the effect that each of the following...Ch. 21 - Describe the effect that each of the following...Ch. 21 - What is an extremophile?Ch. 21 - What are two common environmental settings where...Ch. 21 - Indicate whether each of the following pairings of...Ch. 21 - Indicate whether each of the following pairings of...Ch. 21 - Prob. 21.57EPCh. 21 - What type(s) of extremophiles are used in oil well...Ch. 21 - Prob. 21.59EPCh. 21 - Prob. 21.60EPCh. 21 - Prob. 21.61EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Prob. 21.63EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Prob. 21.65EPCh. 21 - Indicate whether each of the following statements...Ch. 21 - Prob. 21.67EPCh. 21 - Prob. 21.68EPCh. 21 - Prob. 21.69EPCh. 21 - Prob. 21.70EPCh. 21 - Prob. 21.71EPCh. 21 - Prob. 21.72EPCh. 21 - Prob. 21.73EPCh. 21 - Prob. 21.74EPCh. 21 - Prob. 21.75EPCh. 21 - Prob. 21.76EPCh. 21 - Prob. 21.77EPCh. 21 - Prob. 21.78EPCh. 21 - Prob. 21.79EPCh. 21 - Prob. 21.80EPCh. 21 - Prob. 21.81EPCh. 21 - Prob. 21.82EPCh. 21 - What is the medical diagnostic value associated...Ch. 21 - Prob. 21.84EPCh. 21 - Indicate whether each of the following is a...Ch. 21 - Indicate whether each of the following is a...Ch. 21 - Prob. 21.87EPCh. 21 - Prob. 21.88EPCh. 21 - Prob. 21.89EPCh. 21 - Prob. 21.90EPCh. 21 - Prob. 21.91EPCh. 21 - What are the structural differences between the...Ch. 21 - Prob. 21.93EPCh. 21 - Prob. 21.94EPCh. 21 - Vitamin C is biosynthesized in a two-step process....Ch. 21 - Prob. 21.96EPCh. 21 - Prob. 21.97EPCh. 21 - Prob. 21.98EPCh. 21 - Prob. 21.99EPCh. 21 - Prob. 21.100EPCh. 21 - Which of the B vitamins has a structure that fits...Ch. 21 - Which of the B vitamins has a structure that fits...Ch. 21 - Prob. 21.103EPCh. 21 - Prob. 21.104EPCh. 21 - Prob. 21.105EPCh. 21 - Prob. 21.106EPCh. 21 - The coenzyme forms of B vitamins are involved in...Ch. 21 - The coenzyme form of B vitamins are involved in...Ch. 21 - Prob. 21.109EPCh. 21 - What is the relationship between the plant pigment...Ch. 21 - Prob. 21.111EPCh. 21 - List four major functions of vitamin A in the...Ch. 21 - Prob. 21.113EPCh. 21 - Prob. 21.114EPCh. 21 - Prob. 21.115EPCh. 21 - Prob. 21.116EPCh. 21 - Prob. 21.117EPCh. 21 - Prob. 21.118EPCh. 21 - Prob. 21.119EPCh. 21 - Prob. 21.120EPCh. 21 - Which structural form of vitamin E exhibits the...Ch. 21 - Prob. 21.122EPCh. 21 - Prob. 21.123EPCh. 21 - Prob. 21.124EPCh. 21 - Prob. 21.125EPCh. 21 - Prob. 21.126EPCh. 21 - Prob. 21.127EPCh. 21 - Prob. 21.128EPCh. 21 - Prob. 21.129EPCh. 21 - Prob. 21.130EPCh. 21 - Prob. 21.131EPCh. 21 - Which vitamin or vitamins has (have) each of the...Ch. 21 - Which of the 13 vitamins has a structure that fits...Ch. 21 - Prob. 21.134EP
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- The Lineweaver-Burk plot, which illustrates the reciprocal of the reaction rate (1/v) versus the reciprocal of the substrate concentration (1/[S]), is a graphical representation of enzyme kinetics. This plot is typically used to determine the maximum rate, Vmax, and the Michaelis constant, Km, which can be gleaned from the intercepts and slope. Identify each intercept and the slope in terms of the constants Vmax and Km. What term is represented by C? Linewegver-Burk Pt 1/Vmax O A. В. -1/Km Km/Vmax C.arrow_forwardThe Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. Vmax [S] Km + [S] where v is the velocity, or rate, Vmax is the maximum velocity. K 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 (ro) at different substrate concentrations ([S]). First, move the line labeled Vmax to a position that represents the maximum velocity of the enzyme. Next, move the line labeled 1/2 Vmax to its correct position. Then, move the line labeled Km to its correct position. Estimate the values for Vmax and Km- Vmax= µM/min v (µM/min) 300 275 250 225 200 175 150 125 100 75 50 Km = 25 K 0 10 20 30 V max 40 50 [S] (M) 1/2 V max Michaelis-Menten curve 60 70 80 90 100 HMarrow_forwardThe table below lists experimental conditions that can be applied to a reaction catalyzed by a hypothetical Michaelis–Menten enzyme. For each experimental condition described, complete the table to indicate as precisely as possible the effect (no change, half as large doubles, increases, decreases) on the maximal velocity, Vmax, and Michaelis constant, KM, of the hypothetical enzyme.arrow_forward
- 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 V values for the inhibited and uninhibited reactions? Is the inhibitor competitive or max noncompetitive? [S] (mM) V, No Inhibitor (mmol min-') V, Inhibitor Present (mmol min-') 1× 10-4 5 × 10-4 1.5 × 10-3 2.5 × 10-3 5 × 10-3 0.026 0.092 0.136 0.150 0.010 0.040 0.086 0.120 0.165 0.142 Activatearrow_forwardEnzyme X can be inhibited by two distinct inhibitors, only one of which is acting as a competitive inhibitor, while the other one is non-competitive. The three plots below (designated A, B, and Cy show Michaelis-Menten kinetics for the reactions carried out with the same concentr ation of the enzyme and either in the absence of any inhibitors or in the presence of one of the two inhibitors. Match the type of reaction (uninhibited, competitive inhibition, non-competitive inhibition) with the corresponding plot? Plot A Plot B Plot C Substrate concentration 1.Plot A v LUninhibited roaction 2. Plot C v Inhibition by a competitive inhibitor 3Plot B v Inhibition by a non-competitive inhibitor A Moving to another question will save this response. luparrow_forwardDraw Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and Vmax values for the inhibited and uninhibited rxns? Is the inhibitor competitive or noncompetitive? [S] (M) 10,000 1 x 104 2.000-5 x 104 666673 1.5 x 10-3 400- 2.5 x 10-³ 2005x103 V, No Inhibitor (Arbitrary units) 0.026 38,461 0.092 10.87 37100 0.136 7.35 Wak 0.150 -67 0.165 6.06 L slope: 0033 yint=5057 полесте um.x=0.198 km 6.5x 10-4 0.010 0.040 25 10.086 11.63 0.120 8.33 0.142 7.04 2500 V, Inhibitor Present (Arbitrary Units) 100 ↓ $op.= .009 yint: 5.21 900x12 km: 1.73 y/o conf. V10-3 321000arrow_forward
- From a series of flasks with a constant concentration of enzyme the following initial velocities weretaken, they were obtained as a function of the concentration of the substrate.a) Calculate the KM and Vmax kinetic parameters of the three forms (Lineweaver-Burk, Eadie-Hofstee, Dixon).b) Analyze which are the atypical data that cause a low correlation, which can be eliminated and explain youranswer.arrow_forward82.15arrow_forwardMost of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: (a) Lineweaver-Burk equation is a manipulation of the Michaelis-Menten equation. Give the equation and state why it is necessary. (b) Is high or low Vmax preferable for an enzyme reaction? Give reason.arrow_forward
- The rate of an enzyme-catalysed reaction was measured in the absence or presence of a non-competitive inhibitor. Which of the following Lineweaver-Burk plots would you expect to see? a. (a) b. (b) c. (c) d. (d)arrow_forwardDuring the early stages of an enzyme purification protocol, when cells have been lysed but cytosolic components have not been separated, the reaction velocity-versus-substrate concentration is sigmoidal. As you continue to purify the enzyme, the curve shifts to the right. Explain your results. This is an allosteric enzyme and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly. This is an enzyme that displays Michaelis-Menten kinetics and you purify away an inhibitor. This is an allosteric enzyme and during purification you purify away an activator. This is an allosteric enzyme displaying a double-displacement mechanism and during purification you purify away one of the substrates: This is an enzyme that displays Michaelis-Menten kinetics, and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly.arrow_forwardThe following questions deal with a fundamental understanding of enzyme catalysis.a. Why is the rate of an enzyme-catalyzed reaction proportional to the amount of (ES) complex?b. What do you think is meant by saturation of the enzyme?c. What do you think is meant by the term “saturation kinetics”?d. How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reachesa maximum value at high [S]?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSONBiology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStaxAnatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
- Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & CompanyLaboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:9780815344322
Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:W. W. Norton & Company
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.
Inquiry Into Life (16th Edition)
Biology
ISBN:9781260231700
Author:Sylvia S. Mader, Michael Windelspecht
Publisher:McGraw Hill Education
Biomolecules - Protein - Amino acids; Author: Tutorials Point (India) Ltd.;https://www.youtube.com/watch?v=ySNVPDHJ0ek;License: Standard YouTube License, CC-BY