Essential Organic Chemistry, Global Edition
3rd Edition
ISBN: 9781292089034
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Chapter 18.5, Problem 8P
Draw the mechanism for the hydroxide-ion-catalyzed cleavage of fructose-1,6-bisphosphate.
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Chapter 18 Solutions
Essential Organic Chemistry, Global Edition
Ch. 18.1 - Prob. 1PCh. 18.2 - If H218O were used to hydrolyze lysozyme, which...Ch. 18.3 - Which of the following amino acid side chains can...Ch. 18.3 - Arginine and lysine side chains fit into trypsins...Ch. 18.4 - Which of the following amino acid side chains can...Ch. 18.4 - Prob. 6PCh. 18.5 - Prob. 7PCh. 18.5 - Draw the mechanism for the hydroxide-ion-catalyzed...Ch. 18.5 - What advantage does the enzyme gain by forming an...Ch. 18.7 - Prob. 10P
Ch. 18.7 - Prob. 11PCh. 18.8 - How many conjugated double bonds are there in a....Ch. 18.8 - Instead of adding to the 4a-position and...Ch. 18.8 - In succinate dehydrogenase, FAD is covalently...Ch. 18.8 - Prob. 15PCh. 18.9 - Acetolactate synthase is another TPP-requiring...Ch. 18.9 - Acetolactate synthase can also transfer the acyl...Ch. 18.9 - Prob. 18PCh. 18.9 - Prob. 19PCh. 18.10 - Prob. 21PCh. 18.11 - Prob. 23PCh. 18.11 - Which compound is more easily decarboxylated?Ch. 18.11 - Explain why the ability of PLP to catalyze an...Ch. 18.11 - Explain why the ability of PLP to catalyze an...Ch. 18.12 - What groups are interchanged in the following...Ch. 18.13 - Why is the coenzyme called tetrahydrofolate?Ch. 18.13 - What amino acid is formed by the following...Ch. 18.13 - How do the structures of tetrahydrofolate and...Ch. 18.13 - What is the source of the methyl group in...Ch. 18 - Prob. 32PCh. 18 - Prob. 33PCh. 18 - From what vitamins are the following coenzymes...Ch. 18 - Prob. 35PCh. 18 - For each of the following reaction, name both the...Ch. 18 - Explain why serine proteases do not catalyze...Ch. 18 - Prob. 38PCh. 18 - For each of the following enzyme catalyzed...Ch. 18 - Trisephosphate isomerase (TIM) catalyzes the...Ch. 18 - Prob. 41PCh. 18 - What acyl groups have we seen transferred by...Ch. 18 - When UMP is dissolved in T2O, exchange of T for H...Ch. 18 - Prob. 44PCh. 18 - When transaminated, the three branched-chain amino...Ch. 18 - Aldolase shows no activity if it is incubated with...
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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_forwardIf 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 guanylatearrow_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_forward
- Fructose in its bβ - D - pyranose form accounts for the powerful sweetness of honey. The β - D - furanose form, although sweet, is not as sweet as the pyranose form. The furanose form is the more stable form. Draw the two forms and explain why it may not always be wise to cook with honey.arrow_forwardWrite the mechanism for the base-catalyzed conversion of d-fructose to d-glucose and d-mannose.arrow_forwarddoes structure E represent fructofuranose? explainarrow_forward
- Define homolysis or homolytic cleavage ?arrow_forwardPlease 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_forwardPropose a mechanism for the formation of fructose-1,6-bisphosphate from dihydroxyacetone phosphate and glyceraldehyde-3-phosphate, using hydroxide ion as the catalyst.arrow_forward
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