EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
7th Edition
ISBN: 9780100853188
Author: STOKER
Publisher: YUZU
expand_more
expand_more
format_list_bulleted
Concept explainers
Textbook Question
Chapter 21, Problem 21.42EP
Based on the graphical information in Problem 21-41 about enzymes A and B
- a. What is the optimum pH for enzyme B?
- b. What is the optimum temperature for enzyme A?
- c. Which enzyme has the greater activity at a pH of 7.2?
- d. Which enzyme has the greater activity at a temperature of 37.2°C?
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
During a test of kinetics of an enzyme-catalyzed reaction, the following data were recorded:
a. Determine the Michaelis-Menten constant for the reaction with no inhibitor present at 30 °C and at 49.6 °C.
b. Determine the maximum velocity of the uninhibited reaction at 30 °C and an enzyme concentration of 1.6 g/L.
c. Determine the Ki for the inhibitor at 30 °C and decide what type of inhibitor is being used.
a. Estimate KM and Vmax for the uninhibited reaction from the first graph. Whatdifficulties do you find in getting accurate values?b. Make a Lineweaver-Burk (double reciprocal) plot to determine KM and Vmax again.What advantages do you see with the second method? c. Use the Lineweaver-Burk method and the table of data for the inhibitors to determine the kind of inhibition for each inhibitor.
a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve.
b. Provide the type of inhibition for both?
Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3).
d. Calculate the reaction Kcat for the Control in experiment (1).
e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax
and Ky for the enzyme.
c.
(1) V.
[(umol/(ml.s)]
7.6
(2) V-
Τ (μmol/ (ml.s)]
[S] (mM)
(3) V.
[(umol/(ml.s)]
6.6
2
4
14.6
26.6
45.8
4.4
8.6
16.4
29.8
11.4
17.8
24.6
28.2
16
24
60
40.8
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
- a. What is the Vmax of this enzyme WITHOUT inhibitor? Please show your work. b. What is the Km of this enzyme WITHOUT inhibitor? Please show your work. c. The specificity constant of enzyme X is 8 x 10^7 /(M * seconds) What is the kcat of enzyme X WITHOUT inhibitor? Please show your work d. What was the concentration of enzyme used for measuring the kinetics of enzyme X WITHOUT inhibitor? Please show your workarrow_forwardWhat does the Michalis-Menten equation tell you? A. The velocity of an enzyme under physiological conditions B. The variation of enzyme activity as a function of [substrate] C. The quantity of reactant that disappears per unit time D. A and B E. B and C Vo = Vmax [S] KM + [S] Vo = Vmax® [S] KM + [S]arrow_forwardL(24 points) Explain How is the Michaelis constant defined. and what does a low or high value for Km tell you? What is the difference between the velocity and initial velocity of an enzyme reaction? What determines the efficiency of an enzyme reaction, and what terms are used to describe it? 2. (50 points) About how to obtain kinetic data experimentally Lisa decides to obtain values for the Km and Vmax of an enzyme she has just isolated from liver cells (it is now pure), using a Michaelis Menten plot. Describe in detail what kinds of measurements she would have to make, and what she would need to plot on graphs in order to estimnte the values for Km and Vmax. (Show the kinds of graphs she would have to plot, and how these will allow her to estimate Km and Vmax.) Describe how she would be able to obtain Vmax experimentally and from the Michaelis Menten plot - what conditions are needed and what would be measured). Also, describe what she would have to do to obtain the turnover number of…arrow_forward
- Sucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…arrow_forwardThe enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"arrow_forward4) Enzyme 1 and 2 catalyze the same reaction. Both enzymes have the same Km, but Enzyme 1 has a higher Vmax. A. Sketch out what both enzymes look like in a lineweaver burk plot. B. You test an inhibitor (compound A) on both enzymes. In Enzyme 1 The apparent Km increases, in enzyme 2 both the Km and Vmax decrease. What does this suggest about what kind of inhibitor compound A is in each enzyme?arrow_forward
- The 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_forwardcolumns) and absence (second column = control) of enzyme inhibitor. Both inhibitors were added in each reaction at a concentration of 2 mM. The enzyme concentration was similar in all and was approximately 0.001 Им. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and Ky for the enzyme a. C. e. [S] (mM) (1) V. {(umol/(ml.s)] (2) V. [[umol/(ml.s)]| 4.4 (3) V. umol/{ml.s] 6.6 11.4 76 14.6 8.6 26.6 16.4 29 8 17.8 24.6 28.2 16 45.8 24 60 40.8arrow_forwardwhat is the purpose of staggering the start and stop of the reactions? With reference to your experimental protocol, what is the purpose of staggering the start and stop of the reactions? A.To ensure that the reaction occurs with different amounts of enzyme in each tube so as to ensure comparability between reaction tubes. B.To ensure that the reaction occurs at exactly the same pH in each tube so as to ensure comparability between reaction tubes. C.To ensure that the reaction occurs for exactly the same time interval (30 minutes) in each tube so as to ensure comparability between reaction tubes. D.To ensure that the reaction occurs with exactly the same amount of substrate in each tube so as to ensure comparability between reaction tubes.arrow_forward
- Give an example of a noncompetitive inhibitor and its target enzyme. Draw a hypothetical Michaelis-Menten curves in the presence and absence of the noncompetitive inhibitor. Discuss the effects of noncompetitive inhibition and the reasons for these effects on the values of Km and Vmax.arrow_forwardAn enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.arrow_forwardA biochemist wants to determine the effect of inhibitor A to enzyme B which catlyzes the conversion of C to D. The effect of A to the rate of formation of D is shown below: 1. The Km (report to the nearest whole number) for the enzyme-catalyzed reaction in the absence of inhibitor A is _____ mM. 2. The Km for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM. 3. The Vmax for the enzyme catalyzed reaction in the absence of inhibitor A is ____ mM/min 4. The Vmax for the enzyme catalyzed reaction in the presence of inhibitor A is ____mM/min 5. Inhibitor A is a/an ________ inhibitor of enzyme Barrow_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
DIGESTER-35 | VITAMINS AND THEIR RELATED COENZYMES| GPAT | NIPER | PHARMACIST| DI; Author: GPAT DISCUSSION CENTER;https://www.youtube.com/watch?v=CGrdNYmho0s;License: Standard YouTube License, CC-BY