Organic Chemistry, Books a la Carte Edition (8th Edition)
8th Edition
ISBN: 9780134074580
Author: Bruice, Paula Yurkanis
Publisher: PEARSON
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Chapter 22.13, Problem 27P
Interpretation Introduction
Interpretation: The reason why during glycolysis,
Concept introduction:
- Enzyme is a protein that is a biological catalyst. The reactant in a reaction catalyzed by the enzyme is called substrate. In the enzyme, a pocket like cleft is present called active site where it binds the substrate.
- Some amino acid chains in the enzyme act as base, acid and nucleophilic catalyst. Many of the enzymes contain metal ions at the active site which acts as catalyst.
- Acid Catalyst helps in increasing the rate of a particular reaction by the donation of a proton to substrate.
- Base Catalyst helps in increasing the rate of a particular reaction by the removal of a proton to substrate.
- Nucleophilic catalysis helps in increasing the rate of a particular reaction by the formation of a covalent bond with substrate
- Glycolysis: A series of reactions where glucose is converted to two pyruvate molecules in the presence of enzymes catalysis.
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(a) Are galactose and mannose constitutional isomers or stereoisomers? (b) Draw the structure of galactose 1-phosphate and mannose 6-phosphate. (c) Are these two phosphates constitutional isomers or stereoisomers?
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
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
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...
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- One of the steps in the pentose phosphate pathway for glucose catabolism is the reaction of xylulose 5-phosphate with ribose 5-phosphate in the presence of a transketolase to give glyceraldehyde 3-phosphate and sedoheptulose 7-phosphate. (a) The first part of the reaction is nucleophilic addition of thiamin diphosphate (TPP) ylide to xylulose 5-phosphate, followed by a retro-aldol cleavage to give glyceraldehyde 3-phosphate and a TPPcontaining enamine. Show the structure of the enamine and the mechanism by which it is formed. (b) The second part of the reaction is addition of the enamine to ribose 5-phosphate followed by loss of TPP ylide to give sedoheptulose 7-phosphate. Show the mechanism.arrow_forwardThe rate-limiting step is a metabolic pathway is the slowest step which determines the overall rate of the other reactions in the pathway. In glycolysis, the rate limiting step is a phosphorylation reaction where phosphofructokinase (PFK-1) catalyzes the reaction fructose-6-bisphosphate -> fructose-1,6-bisphosphate, the same step in gluconeogenesis. Select one: The statement is FALSE. The statement is TRUE.arrow_forwardThe enzyme 6-phosphogluconate dehydrogenase is part of the pentose pathway for glucose oxidation. What enzyme that is involved in glucose oxidation by the citric acid cycle has a very similar reaction mechanism to 6-phosphogluconate dehydrogenase? A) isocitrate dehydrogenase B) alpha-ketoglutarate dehydrogenase C) succinate dehydrogenase D) malate dehydrogenase E) pyruvate dehydrogenase (99+ RATI aarrow_forward
- 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_forwardWhen d-glucose is reduced with sodium borohydride, optically active glucitol results.When optically active d-galactose is reduced, however, the product is optically inactive.Explain this loss of optical activityarrow_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_forward
- β-D-N-acetylgalactosamine and α-D-N-acetylglucosamine are examples of epimers, enantiomers, aldose-ketose pair, or anomers?arrow_forwardA ketose can be converted to an aldose through an enediol intermediate. What is the structure of the enediol intermediate when D-fructose is converted to D-glucose?arrow_forwardNonearrow_forward
- What structural feature is required for a carbohydrate to behave asreducing sugar?arrow_forwardWhat structures are produced by the epimerization of galactose?arrow_forwardWhat is the product of the reaction when α-amylase acts on amylose? (A) amylose molecules (B) monosaccharide molecules (C) different-sized oligosaccharide fragments (D) different-sized polysaccharide fragmentsarrow_forward
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