Organic Chemistry (8th Edition)
Organic Chemistry (8th Edition)
8th Edition
ISBN: 9780134042282
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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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.)

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5. In the subsequent stages of glycolysis (see figure below): (1) cleavage of FBP to dihydroxyacetone (DHP) and glyceraldehyde 3-phosphate (G3P) according to FBP → DHP + G3P is catalyzed by aldolase with K₁ = 104 and (2) the DHP and G3P can interconvert (DHP → G3P), a process catalyzed by triose phosphate isomerase with K₂ = 0.040. If a 1.75 mM solution of FBP is treated with both of these enzymes (enabling both of these reactions) at pH 7 and 37°C, find the resulting equilibrium concentration of each species.
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
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 (8th Edition)

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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