Organic Chemistry, Books a la Carte Edition (8th Edition)
8th Edition
ISBN: 9780134074580
Author: Bruice, Paula Yurkanis
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 22, Problem 42P
Proof that an imine was formed between aldolase and its substrate was obtained by using D-fructose-1,6-bisphosphate labeled at the C-2 position with l4C as the substrate. NaBH4 was added to the reaction mixture. A radioactive product was isolated from the reaction mixture and hydrolyzed in an acidic solution. Draw the structure of the radioactive product obtained from the acidic solution. (Hint: NaBH4 reduces an imine linkage.)
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
If an enzyme-catalyzed reaction has a high rate at low pH and low rate at higher
pH, this implies that a group on either the enzyme or the substrate must be
for an efficient reaction.
leaving group
oxidoreductase
coenzymes
O protonated
deprotonated
The compound that consists of deoxyribose linked by an N-glycosidic bond to
N-9 of guanine is:
adenylate
deoxyguanosine
guanosine
nucleotide
guanylate
what is the structure digested by and how many
reducing sugars are present
ОН ОН
Но
OH
HO
Но
HO-
OH
HO,
The trisaccharide pictured could be completely digested (ie into monomers) by
a beta-galactosidase and an alpha-glucosidase
an alpha-galactosidase and sucrase
lactase and sucrase
a beta-fructosidase and lactase
4. The AGo for the aldolase reaction is 22.8 kJ/mol. When the reaction is run in a hepatocyte cell at
37°C, the concentrations of the intermediates are: fructose 1,6-bisphosphate =1.41 x 103 M,
glyceraldehyde 3-phosphate 2.95 x 10-6 M, and dihydroxyacetone phosphate = 1.62 x 10-5 M.
Calculate the free energy change for this reaction
Is this reaction thermodynamically favorable
Chapter 22 Solutions
Organic Chemistry, Books a la Carte Edition (8th Edition)
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
- TPP is a coenzyme for transketolase, the enzyme that catalyzes the conversion of a ketopentose (xylulose5-phosphate) and an aldopentose (ribose-5-phosphate) to an aldotriose (glyceraldehyde-3-phosphate) and a ketoheptose (sedoheptulose-7-phosphate). Notice that the total number of carbons in the reactants and products is the same (5 + 5 = 3 + 7). Propose a mechanism for this reaction.arrow_forwardTPP is a coenzyme for transketolase, the enzyme that catalyzes the conversion of a ketopentose (xylulose- 5-phosphate) and an aldopentose (ribose-5-phosphate) to an aldotriose (glyceraldehyde-3-phosphate) anda ketoheptose (sedoheptulose-7-phosphate). Notice that the total number of carbons in the reactants and products is the same (5 + 5 = 3 + 7). Propose a mechanism for this reaction.arrow_forwardThe following figure shows the intermediate of the transketolase mechanism. Use arrow pushing to form the resonance stabilized enzyme intermediate. Show the mechanism for reaction of this intermediate with the given aldose, using the protonated acid/base residue suppliec by the enzyme. Clearly show the product of the reaction and make sure that the acid/base residue ends up in the protonated state at the end or your mechanism. H. CH,OH H-B H- HO- OH H- OH CH,OPO,arrow_forward
- Using this information and the image provided, describe the reaction catalyzed by an esterase and classify it as one of the 6 classes of enzymes. The insert also tells you that Enalaprilat (the active form of Enalapril) targets angiotensin-converting enzyme (ACE), which cleaves the blood-pressure regulating peptide angiotensin I. The active form of the drug looks very similar to the endogenous substrate of the enzyme ACE. Based on this information, what type of interaction is occurring between Enalaprilat and ACE? Propose how the presence of Enalaprilat changes the overall reaction.arrow_forwardOne of the steps in the pentose phosphate pathway for glucose catabolism is the reaction of sedoheptulose 7-phosphate with glyceraldehydes 3-phosphate in the presence of a transaldolase to yield erythrose 4-phosphate and fructose 6-phosphate. (a) The first part of the reaction is the formation of a protonated Schiff base of sedoheptulose 7-phosphate with a lysine residue in the enzyme followed by a retro-aldol cleavage to give an enamine plus erythrose 4-phosphate. Show the structure of the enamine and the mechanism by which it is formed. (b) The second part of the reaction is a nucleophilic addition of the enamine to glyceraldehyde 3-phosphate followed by hydrolysis of the Schiff base to give fructose 6-phosphate. Show the mechanism.arrow_forwardIn the pentose phosphate pathway for degrading sugars, ribulose 5-phosphate is converted to ribose 5-phosphate. Propose a mechanism for the isomerization.arrow_forward
- Please draw by hand. 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 base and an acid catalyst, respectively. Propose a mechanism for the reaction. ОН 2-03Р0 ОН dihydroxyacetone phosphate triosephosphate isomerase 2-03РО. H glyceraldehyde-3-phosphate FYI Glu is glutamic acid and his is histadinearrow_forwardQ11: For the following enzyme catalyzed reaction, indicate where the transition state occurs and whether you expect the enzyme to increase the transition towards the product? Product Reactant Reaction Progression Q12: For the following endergonic reaction, would you expect the presence of malate dehydrogenase to facilitate this reaction proceeding towards oxaloacetate, when both malate and oxaloacetate are present in equimolar amounts? ÇOO- fo0 NAD* COO- NADH + H* Но—с—Н 0=C CH2 CH2 malate CO" COO- dehydrogenase L-Malate Oxaloacetate AG'° = 29.7 kJ/mol AG Free Energyarrow_forwardChorismate mutase is an enzyme that promotes a pericyclic reaction by forcing the substrate to assume the conformation needed for the reaction. The product of the pericyclic reaction is prephenate that is subsequently converted into the amino acids phenylalanine and tyrosine. What kind of a pericyclic reaction does chorismate mutase catalyze?arrow_forward
- In the first step of aminoacyl group linkage to a tRNA, an amino acid reacts with ATP to yield an aminoacyl-AMP and pyrophosphate. The bond between the amino acyl group and the AMP is described as a mixed anhydride. Explain the differences between an anhydride bond and a mixed anhydride bond. Why is this reaction irreversible?arrow_forwardIn the 1st reaction of citric acid cycle, acetyl CoA and oxaloacetate are combined to form citrate as shown below. What is the best way to describe this reaction? CH acetyl Col CH₂ co exaloncertate HO citrate synthase ço, CH₂ HO-C-00 CH₂ co₂ citrate O It begins with an Aldol reaction followed by hydrolysis of CoA thioester). It begins with a keto-enol tautomerization followed by an Aldol reaction. It involves a Claisen condentation. OIt involves an Aldol condensation. None of the abovearrow_forwarda Lactate dehydrogenase H H3C-C-coO- ОН ooc-C-CH3 L-(+)-Lactase Pyruvate This is a(an) b Creatine kinase CH3 O CH3 O H2N, АТР ADP NH2 NH2 Adenosine triphosphate Adenosine diphosphate Creatine Phosphocreatine This is a(an)arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Chemistry & Chemical ReactivityChemistryISBN:9781337399074Author:John C. Kotz, Paul M. Treichel, John Townsend, David TreichelPublisher:Cengage Learning
Chemistry & Chemical Reactivity
Chemistry
ISBN:9781337399074
Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel
Publisher:Cengage Learning
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