EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
7th Edition
ISBN: 8220100853180
Author: STOKER
Publisher: CENGAGE L
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 21, Problem 21.35EP
(a)
Interpretation Introduction
Interpretation: The term absolute specificity has to be defined.
Concept introduction: Enzymes show different types of selectivity for different substrates. The active site of the enzyme determines the enzyme specificity.
(b)
Interpretation Introduction
Interpretation: The term linkage specificity has to be defined.
Concept introduction: Enzymes show different types of selectivity for different substrates. The active site of the enzyme determines the enzyme specificity.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Regarding the physical condition (characteristics of the solution/environment) in which an enzyme finds itself: sometimes enzymes are most active at a certain level and still active but to a lesser degree at a level above or below the optimal level. Describe the likely reason for the enzyme’s decrement in function at levels other than the optimal level?
Two different preparations of the same enzyme are characterized below.
Total protein
(mg)
Total activity
(activity units)
Step
Volume
Specific activity
(ml)
Preparation 1
300
1000
600,000
Preparation 2
200
1000
500,000
a) Fill in the 3 double-underlined blanks on the table below.
b) Which of the 2 preparations would you think is likely to be more pure? Explain.
A multi-enzyme complex Is made up of three polypeptide chains, A, B and C. A is
associated with decarboxylase activity; B is a transacetylase, while C is a
dehydrogenase. When the protein was placed in a nonpolar solvent, then run in
PAGE, two protein bands were observed. Enzyme assays showed that one
protein band exhibited decarboxylase activity while the other has both
transacetylase and dehydrogenase activities. When the protein was also placed
in an aqueous solvent at pH 5.0, then run in electrophoresis, two protein bands
were also detected. Further enzyme assays also showed that one protein band
exhibits transacetytase activity while the other has both decarboxylase and
dehydrogenase activities.
a. What types of non-covalent interactions are possible between A, B and C?
b. Addition of urea, a reducing agent gave 4 bands in the PAGE profile with a
subsequent loss of decarboxylase activity. What could be the reason for the
observed result? Explain briefly in terms of the structure…
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
- Define enzyme denaturation in terms of protein structure. What environmental factors can denature enzymes?arrow_forward200 ml of a 2% protein solution are available, containing an enzyme to be purified. Half of the sample is subjected to method A, consisting of fractionated precipitations, and 5 ml of final solution are obtained, with a protein concentration equal to 5 mg / ml and enzymatic activity equal to 2000 U / ml. The other half is subjected to method B, consisting of ion exchange chromatography, and a final solution of 10 ml is obtained, with a protein richness equal to 10 mg / ml, and with an enzymatic activity equal to 2000 U / ml. You want to know: a) Which of the methods has provided the purest enzyme. b) By which of the methods has the greatest amount of protein been obtained.arrow_forwardOn the figure below are shown three Lineweaver-Burk plots for enzyme reactions that have been carried out in the presence, or absence, of an inhibi- tor. Indicate what type of inhibition is predicted based on each Lineweaver- Burk plot. For each plot indicate which line corresponds to the reaction without inhibitor and which line corresponds to the reaction with inhibitor present. 1 1 1 [S] [S] [S]arrow_forward
- A. Lineweaver-Burk plot of the enzyme with increasing amounts of substrate in the absence or the presence of the inhibitor is shown below. Graph A : x-intercept Graph B : x-intercept = - 0.012, y-intercept = 0.8 Graph C : x-intercept = - 0.027, y-intercept = 0.8 Graph D : x-intercept = - 0.039, y-intercept = 0.8 - 0.007, y-intercept = 0.8 Graph A 4 Graph B Graph C Graph D 1 -0,04 -0,02 0,00 0,02 0,04 1/[Substrate] (uM) (i) Which graph indicates an enzymatic reaction without inhibitor? (ii) Which type of inhibitor is it? Briefly explain. (iii) Which graph indicates the highest concentration of inhibitor? (iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers. 1/Rate (umol/min)arrow_forwardA с Wan WWW GHEDE MAK am2 Increasing CE a-1 (no inhibitor) Slope #KY... ...." 7-15 7 a>c²=1 [no inhibitori Slope R 101 9-19 aver-Burk plots in this figure represent the activities of enzymes in the 4-5 n. 155 B D MIN -a'/KM 0.8- 1/V >~- -1/K 0 01 m(app) d'Nmax a=2 a=1.5 1[S] per mM inhibitor a=10 Slope Karrow_forwardYou have performed protein purification on your new favorite enzyme using a protocol which involves the following steps/samples: crude extract, ammonium sulfate cut, ion exchange and gel filtration. You need to run 25ug of protein from your crude extract sample on an SDS-PAGE gel. You have determined that the protein concentration of your crude extract sample is 2.1mg/ml. Your total sample volume is 30ul. You have water for your diluent and 6x SDS-loading dye to prepare your sample. List the components of your prepared sample. Note: you will only have access to a P20 and a P200 to prepare this sample.arrow_forward
- The manufacture of chocolates containing a liquid center is an interesting application of enzyme engineering. The flavored liquid center consists largely of an aqueous solution of sugars rich in fructose to providesweetness. The technical dilemma is the following: the chocolate coating must be prepared by pouring hot melted chocolate over a solid (or almost solid) core, yet the final product must have a liquid, fructose-rich center. Suggest a way to solve this problem. (Hint: Sucrose is much less soluble than a mixture of glucose and fructose.)arrow_forwardHow temperature, pH and salt affects the enzyme activity in terms of protein structure (primary, secondary, tertiary, quaternary) and other factors? Please explain briefly.arrow_forwardData from enzyme inhibition are used to determine a Kmapp and Vmax PP. Comparison of these values with assays run without inhibitor are used to understand how the inhibition is occurring. This is useful for better understanding the active site as well as the practical aspect of pharmaceutical drugs. Below are idealized Line-Weaver Burke plots of different types of inhibitors. Comnetitive Uncomnetitive Mixed +Inh +Inh 4Inh Anh Inh Anh [S] [S] [S] a. How does the value of Vmax for the enzyme compare to the Vmax PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed b. How does the value of Km for the enzyme compare to the Km PP of the inhibited enzyme for: i. Competitive ii. Uncompetitive iii. Mixed c. For each situation in Model 1, consider an inhibitor that is better than the one shown on the graph. Answer the following questions for each type of inhibition: i. How would the KmPP change? ii. How would the Vmax PP change?arrow_forward
- A hollow fiber enzyme reactor (HFER) consists of 5000 fibers. Each fiber has an internal diameter of 0.04 cm, and on the inside surface of the fibers, an enzyme has been immobilized that removes a toxin from plasma that is flowing through the inside of the fibers. The enzyme reaction is very fast, so a reasonable assumption is that the concentration of the toxin at the surface of the hollow fiber is equal to zero. The /HFER operates at 37°C, and the plasma enters at a total flow rate of 200 mL/min. The concentration of the toxin in the plasma that enters the HFER is 1 mg/L, and its MW is 636 g/mol. If the fibers in the HFER are 50 cm in length, what is the concentration of the toxin in the plasma as it leaves the HFER?arrow_forwardList down the properties of an ideal carrier matrix for enzyme immobilization.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_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