EBK ORGANIC CHEMISTRY
8th Edition
ISBN: 8220102744127
Author: Bruice
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 22.13, Problem 25P
What advantage does the enzyme gain by forming an imine?
Expert Solution & Answer
Trending nowThis is a popular solution!
Students have asked these similar questions
1. What is the role of initiator and inhibitor?
2. What are short stops?
Explain why an irreversible inhibitor of an enzyme might be more toxic to humans than a reversible inhibitor.
FInd the product of this enzyme catalyzed reaction.
Chapter 22 Solutions
EBK ORGANIC CHEMISTRY
Ch. 22.2 - Compare each of the mechanisms listed here with...Ch. 22.2 - Prob. 3PCh. 22.2 - Prob. 4PCh. 22.3 - a. Draw the mechanism for the following reaction...Ch. 22.5 - Prob. 7PCh. 22.5 - Propose a mechanism for the Co2+ catalyzed...Ch. 22.6 - Prob. 9PCh. 22.7 - Prob. 10PCh. 22.7 - Prob. 12PCh. 22.7 - Prob. 13P
Ch. 22.9 - Which of the following amino acid side chains can...Ch. 22.9 - Which of the following C-terminal peptide bonds is...Ch. 22.9 - Carboxypeptidase A has esterase activity as well...Ch. 22.10 - Arginine and lysine side chains fit into trypsins...Ch. 22.10 - Explain why serine proteases do not catalyze...Ch. 22.11 - If H2 18O is used in the hydrolysis reaction...Ch. 22.11 - Draw the pH-activity profile for an enzyme that...Ch. 22.12 - The pHactivity profile for glucose-6-phosphate...Ch. 22.12 - Prob. 23PCh. 22.13 - Draw the mechanism for the hydroxide ion-catalyzed...Ch. 22.13 - What advantage does the enzyme gain by forming an...Ch. 22.13 - Prob. 26PCh. 22.13 - Prob. 27PCh. 22.13 - Aldolase shows no activity if it is incubated with...Ch. 22 - Which of the following parameters would be...Ch. 22 - Prob. 29PCh. 22 - Prob. 30PCh. 22 - Prob. 31PCh. 22 - Indicate the type of catalysis that is occurring...Ch. 22 - The deuterium kinetic isotope effect (KH2O/KD2O)...Ch. 22 - Prob. 34PCh. 22 - Co2+ catalyzes the hydrolysis of the lactam shown...Ch. 22 - there are two kinds of aldolases. Class I...Ch. 22 - Prob. 37PCh. 22 - The hydrolysis of the ester shown here is...Ch. 22 - Prob. 39PCh. 22 - At pH = 12, the rate of hydrolysis of ester A is...Ch. 22 - 2-Acetoxycyclohexyl tosylate reacts with acetate...Ch. 22 - Proof that an imine was formed between aldolase...Ch. 22 - Prob. 43PCh. 22 - a. Explain why the alkyl halide shown here reacts...Ch. 22 - Triosephosphate isomerase (TIM) catalyzes the...
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
- Neostigmine is an inhibitor of acetylcholinesterase. The enzyme attempts to catalyse the same reaction on neostigmine as it does with acetylcholine. However, a stable intermediate is formed which prevents completion of the process and which results in a molecule being covalently linked to the active site. Identify (draw) the stable intermediate and explain why it is stable.arrow_forwardThe hydrolysis of an ester can be sped up by both acidic and basic conditions. Aminolysis of an ester can be sped up by acidic conditions, but not by basic conditions. Explain why.arrow_forwardThe substance where the enzyme reacts with? A. Substrate B. Inhibitor C. A & B D. Activator E. Productarrow_forward
- Oxaloacetate is an inhibitor of succinate dehydrogenase because it is structurally very similar to succinate as shown below. Also, its binding to the enzyme does not involve any covalent bond formation. What type of inhibitor is oxaloacetate? COO | CH₂ 1 CH₂ 1 COO Succinate COO | CH₂ C=O COO Oxaloacetate O a noncompetitive inhibitor both a noncompetitive and an irreversible inhibitor O an irreversible inhibitor O a competitive inhibitorarrow_forwardFind the product of this enzyme catalyzed reaction.arrow_forwardWhat is an antioxidant enzyme? Why is catalase considered to be an antioxidant enzyme?arrow_forward
- Am I correct? Please helparrow_forwardI don't get it at all my homework. I struggled with this question. Can you help me? Can you explain to me?arrow_forwardSubstrates are held in place at the active site of an enzyme with: A. Weak, noncovalent, reversible interactions B. Strong, covalent, reversible interactions C. Weak, noncovalent, irreversible interactions D. Weak, covalent, reversible interactionsarrow_forward
- Triosephosphate isomerase (TIM) catalyzes the conversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate. The enzyme’s catalytic groups are Glu 165 and His 95. In the first step of the reaction, these catalytic groups function as a general-base and a general-acid catalyst, respectively. Propose a mechanism for the reaction.arrow_forwardDraw the structures of the substrate (pNPP) and of the inhibitors (Pi and Phe). Consider them in the fully deprotonated states. What similarities can you detect between each inhibitor and the substrate?arrow_forwardActivation of a zymogen is by covalent modification. How might phosphorylation or dephosphorylation (also covalent modification) modify an enzyme to make it more active (or more inactive)?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Introductory Chemistry: A FoundationChemistryISBN:9781337399425Author:Steven S. Zumdahl, Donald J. DeCostePublisher:Cengage Learning
Chemistry for Today: General, Organic, and Bioche...ChemistryISBN:9781305960060Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. HansenPublisher:Cengage Learning
General, Organic, and Biological ChemistryChemistryISBN:9781285853918Author:H. Stephen StokerPublisher:Cengage Learning
Organic And Biological ChemistryChemistryISBN:9781305081079Author:STOKER, H. Stephen (howard Stephen)Publisher:Cengage Learning,
World of Chemistry, 3rd editionChemistryISBN:9781133109655Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCostePublisher:Brooks / Cole / Cengage Learning
World of ChemistryChemistryISBN:9780618562763Author:Steven S. ZumdahlPublisher:Houghton Mifflin College Div
Introductory Chemistry: A Foundation
Chemistry
ISBN:9781337399425
Author:Steven S. Zumdahl, Donald J. DeCoste
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
General, Organic, and Biological Chemistry
Chemistry
ISBN:9781285853918
Author:H. Stephen Stoker
Publisher:Cengage Learning
Organic And Biological Chemistry
Chemistry
ISBN:9781305081079
Author:STOKER, H. Stephen (howard Stephen)
Publisher:Cengage Learning,
World of Chemistry, 3rd edition
Chemistry
ISBN:9781133109655
Author:Steven S. Zumdahl, Susan L. Zumdahl, Donald J. DeCoste
Publisher:Brooks / Cole / Cengage Learning
World of Chemistry
Chemistry
ISBN:9780618562763
Author:Steven S. Zumdahl
Publisher:Houghton Mifflin College Div
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