Introduction to General, Organic and Biochemistry
11th Edition
ISBN: 9781285869759
Author: Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Question
Chapter 23, Problem 23.28P
Interpretation Introduction
Interpretation:
Using the given data, whether inhibition by 2 m urea is competitive or noncompetitive is to be determined.
Concept introduction:
Competitive inhibition occurs when a substance that is not the substrate of the enzyme under normal condition can also bind to the enzyme’s active site. This results in direct competition with the substrate for the active site. Noncompetitive inhibition occurs when an inhibitor binds to a site present on the enzyme that is distinct from the active site which causes an alteration in the shape of the active site, making it unavailable for the substrate.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
An 90 kg subject consumed a snack that contained 80 g of carbohydrate. Before eating the snack the subject’s blood glucose was 6.0 mmol.L-1. Calculate the concentration of glucose (mM) that would be reached in the blood after consuming the snack.Assume that all the carbohydrate in the snack was converted to glucose, rapidly absorbed and distributed throughout the extracellular water (ECW) within 30 minutes. Assume ECW is approximately 20% of body weight and the glucose is not metabolised further.
Consider a drug molecule that binds to an enzyme with a Kd of 20.281 nM. If the intracellular concentration of the free drug in a patient is 19.225 nM at equilibrium, what percentage of enzyme molecules are bound to the drug?
The activation energy needed for a biochemical reaction is decreased by .....
Group of answer choices
a. a product
b. an enzyme
c. a change in temperature
d. a substrate
Chapter 23 Solutions
Introduction to General, Organic and Biochemistry
Ch. 23 - What is the difference between a catalyst and an...Ch. 23 - What are ribozymes made of?Ch. 23 - Would a lipase hydrolyze two triglycerides, one...Ch. 23 - Compare the activation energy in uncatalyzed...Ch. 23 - Prob. 23.5PCh. 23 - Prob. 23.6PCh. 23 - Prob. 23.7PCh. 23 - Monoamine oxidases are important enzymes in brain...Ch. 23 - Prob. 23.9PCh. 23 - 0 What kind of reaction does each of the following...
Ch. 23 - Prob. 23.11PCh. 23 - Prob. 23.12PCh. 23 - 3 What is the difference between reversible and...Ch. 23 - Prob. 23.14PCh. 23 - 5 At a very low concentration of a certain...Ch. 23 - 6 If we wish to double the rate of an...Ch. 23 - 7 A bacterial enzyme has the following...Ch. 23 - 8 The optimal temperature for the action of...Ch. 23 - 9 The activity of pepsin was measured at various...Ch. 23 - Prob. 23.20PCh. 23 - Prob. 23.21PCh. 23 - Prob. 23.22PCh. 23 - Prob. 23.23PCh. 23 - 4 What kind of chemical reaction occurs most...Ch. 23 - 5 Which of the following is a correct statement...Ch. 23 - Prob. 23.26PCh. 23 - 7 Enzymes are long protein chains, usually...Ch. 23 - Prob. 23.28PCh. 23 - Prob. 23.29PCh. 23 - 0 Can the product of a reaction that is part of a...Ch. 23 - 1 What is the difference between a zymogen and a...Ch. 23 - 2 The enzyme trypsin is synthesized by the body in...Ch. 23 - Prob. 23.33PCh. 23 - Prob. 23.34PCh. 23 - Prob. 23.35PCh. 23 - Prob. 23.36PCh. 23 - Prob. 23.37PCh. 23 - Prob. 23.38PCh. 23 - 9 The enzyme phosphofructokinase (PFK) (Chapter...Ch. 23 - Prob. 23.40PCh. 23 - 1 After a heart attack, the levels of certain...Ch. 23 - Prob. 23.42PCh. 23 - Prob. 23.43PCh. 23 - Prob. 23.44PCh. 23 - 5 Chemists who have been exposed for years to or...Ch. 23 - 6 Which enzyme preparation is given to patients...Ch. 23 - 7 Chymotrypsm is secreted by the pancreas and...Ch. 23 - 8 Explain why transition-state analogs are potent...Ch. 23 - Prob. 23.49PCh. 23 - 0 Explain the relationship between...Ch. 23 - 1 (Chemical Connections 23A) Acetylcholine causes...Ch. 23 - Prob. 23.52PCh. 23 - Prob. 23.53PCh. 23 - Prob. 23.54PCh. 23 - Prob. 23.55PCh. 23 - 6 (Chemical Connections 23C) What role does Mn2+...Ch. 23 - 7 (Chemical Connections 23C) Which amino acids of...Ch. 23 - 8 (Chemical Connections 23D) What is the strategy...Ch. 23 - 9 (Chemical Connections 23D) Why did scientists...Ch. 23 - Prob. 23.60PCh. 23 - Prob. 23.61PCh. 23 - Prob. 23.62PCh. 23 - 3 (Chemical Connections 23E) What is the...Ch. 23 - Prob. 23.64PCh. 23 - Prob. 23.65PCh. 23 - Prob. 23.66PCh. 23 - Prob. 23.67PCh. 23 - Prob. 23.68PCh. 23 - Prob. 23.69PCh. 23 - Prob. 23.70PCh. 23 - 1 Food can be preserved by inactivation of enzymes...Ch. 23 - Prob. 23.72PCh. 23 - 3 Would you expect to find active digestive...Ch. 23 - Prob. 23.74PCh. 23 - Prob. 23.75PCh. 23 - Prob. 23.76PCh. 23 - 7 An enzyme has the following pH dependence: At...Ch. 23 - Prob. 23.78PCh. 23 - Prob. 23.79PCh. 23 - 0 Nerve gases operate by forming covalent bonds at...Ch. 23 - 1 What would be the appropriate name for an enzyme...Ch. 23 - Prob. 23.82PCh. 23 - 3 A liver enzyme is made of four subunits: 2A and...Ch. 23 - Prob. 23.84PCh. 23 - Prob. 23.85PCh. 23 - Prob. 23.86PCh. 23 - Prob. 23.87PCh. 23 - Prob. 23.88PCh. 23 - Prob. 23.89PCh. 23 - Prob. 23.90PCh. 23 - Prob. 23.91P
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_forwardCompare the lock-and-key and induced-fit models for substrate binding to an enzyme.arrow_forwardDescribe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.arrow_forward
- 3) The enzyme aldolase catalyzes the conversion of fructose-1,6-diphosphate (FDP)to dihydroxyacetone phosphate (DHAP) and glyceraldehide-3-phosphate (G3P). Thereaction isFDP ⇄ DHAP + G3P , ∆rG0(298.15 K) = 23.8 kJ mol−1In red blood cells the concentration of these species are [FDP] = 35 µM, [DHAP] =130 µM, and [G3P] = 15 µM. (Remember that 1.0 µM = 1.0 × 10−6 mol L−1. Thestandard state for reactions in solution can be taken as c0 = 1.0 mol L−1).Calculate ∆rG in a red blood cell at 25 0C. Will the reaction occur spontaneouslyin the cell at this temperature?arrow_forwardHow is this reaction sequence regulated? CO2(g) + H2O(l) ⟷ H2CO3(aq) H2CO3(aq) ⟷ H+1(aq) + HCO3-1(aq) Group of answer choices Breathing controls carbon dioxide concentration and carbonic anhydrase catalyzes the reaction to lower the activation energy. Ingestion of nutrients controls carbon dioxide concentration and carbonic anhydrase catalyzes the reaction to lower the activation energy. Breathing controls carbon dioxide concentration and carbonic anhydrase catalyzes the reaction to increase the activation energy. Metabolism controls carbon dioxide concentration and carbonic anhydrase catalyzes the reaction to increase the activation energy. Ingestion of nutrients controls carbon dioxide concentration and carbonic anhydrase catalyzes the reaction to increase the activation energy.arrow_forwardEvery valentine’s day, CVS sells chocolate-covered cherries. The chocolate-covered cherries are like a mini cake with a cherry inside. The cake comprises a combination of sucrose (powder sugar), butter, cherry juice, and an enzyme (invertase). Time (hours) Sucrose Concentration (g/cm3) 0 0.844 24 0.681 48 0.550 96 0.357 192 0.153 While stored at 5.00C, the sucrose hydrolyzes to produce glucose and fructose. The mixture of the glucose and fructose is a liquid called invert sugar. Below you will find the concentration of sucrose in the cake as a function of time. For the cherries to be edible, the 85% of the sucrose must be hydrolyzed. Before you start to answer the question, create a data table that comprises sucrose concentration in units of moles per liter. Write the chemical reaction that demonstrates the hydrolysis of sucrose. With the data, determine how long it will take for 85% of the sucrose to be converted into…arrow_forward
- What is the effect of an enzyme on the activation energy ofa reaction?arrow_forwardGiven enzyme catalyzed reaction k1= 4x106 M-1s-1, k -1=6x104 s-1, k2=2.0x103s-1. Determine if the enzyme-substrate binding follow the equilibrium or not?arrow_forwardQuesrion: Enzyme X exhibits maximum activity at pH = 10.5. X shows a fairly sharp decrease in its activity when the pH goes much lower than 9.5. One likely interpretation of this pH activity is that: a. A His residue on the enzyme is involved in the reaction b. a Glu residue on the enzyme is involved in the reaction c. a Tyr residue on the enzyme is involved in the reaction d. the enzyme uses NADH has a cofactor e. the enzyme uses coenzyme A has a cofactor Please explain why, thanks!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 above diagram illustrates ___? The relationship between the proteome and the metabolome The relationship between the concentration of enzymes and the rate of chemical reactions they catalyze a and barrow_forward384 Enzyme Reactions and Kinetics Q6.3: What kinetic parameter reveals the most information about how well an enzyme works? Describe this kinetic parameter in terms of the turnover number and the Michaelis constant and provide an explanation for why triosephosphate isomerase is considered to be ~16,000 better than pepsin when this kinetic parameter is used to compare these two enzymes.arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
- Chemistry for Today: General, Organic, and Bioche...ChemistryISBN:9781305960060Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. HansenPublisher:Cengage LearningChemistry & Chemical ReactivityChemistryISBN:9781337399074Author:John C. Kotz, Paul M. Treichel, John Townsend, David TreichelPublisher:Cengage LearningOrganic And Biological ChemistryChemistryISBN:9781305081079Author:STOKER, H. Stephen (howard Stephen)Publisher:Cengage Learning,
- General, Organic, and Biological ChemistryChemistryISBN:9781285853918Author:H. Stephen StokerPublisher:Cengage LearningChemistry: The Molecular ScienceChemistryISBN:9781285199047Author:John W. Moore, Conrad L. StanitskiPublisher:Cengage LearningIntroductory Chemistry: A FoundationChemistryISBN:9781337399425Author:Steven S. Zumdahl, Donald J. DeCostePublisher: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:9781337399074
Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Publisher:Cengage Learning
Organic And Biological Chemistry
Chemistry
ISBN:9781305081079
Author:STOKER, H. Stephen (howard Stephen)
Publisher:Cengage Learning,
General, Organic, and Biological Chemistry
Chemistry
ISBN:9781285853918
Author:H. Stephen Stoker
Publisher:Cengage Learning
Chemistry: The Molecular Science
Chemistry
ISBN:9781285199047
Author:John W. Moore, Conrad L. Stanitski
Publisher:Cengage Learning
Introductory Chemistry: A Foundation
Chemistry
ISBN:9781337399425
Author:Steven S. Zumdahl, Donald J. DeCoste
Publisher:Cengage Learning
Chemical Equilibria and Reaction Quotients; Author: Professor Dave Explains;https://www.youtube.com/watch?v=1GiZzCzmO5Q;License: Standard YouTube License, CC-BY