Organic Chemistry (8th Edition)
8th Edition
ISBN: 9780134042282
Author: Paula Yurkanis Bruice
Publisher: PEARSON
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Chapter 22.13, Problem 28P
Aldolase shows no activity if it is incubated with iodoacetic acid before fructose-1.6-bisphosphate is added to the reaction mixture. What causes this loss of activity?
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Aldolase shows no activity if it is incubated with iodoacetic acid before fructose-1,6-bisphosphate is added to the reaction mixture. What causes this loss of activity?
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
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.
Chapter 22 Solutions
Organic Chemistry (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 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 glycolytic pathway, a six-carbon sugar (fructose 1,6-bisphosphate) is cleaved to form two three-carbon sugars, which undergo further metabolism . In this pathway, an isomerization of glucose 6-phosphate tofructose 6-phosphate (shown below) occurs two steps before the cleavage reaction (the intervening step is phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate ). What does the isomerization step accomplish from a chemical perspective? (Hint: Consider what might happen if the C—C bond cleavage were to proceed without the preceding isomerization.)arrow_forward5. 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.arrow_forward
- Nonearrow_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_forwardWhich of the following enzymes catalyzes a reaction with the pictured compound as an intermediate? = Hz C—6 ཆོས་རིག་ག་ག་ག་ག་ག་གས་པ་ 0—P, O succinyl-CoA synthetase fumarase succinate dehydrogenase malate dehydrogenase a-ketoglutarate dehydrogenasearrow_forward
- Draw the product of the following metabolic reaction. HCO3, ATP CH3CSC0A ADP + P₁ + H+ N-Carboxybiotin • Use the wedge/hash bond tools to indicate stereochemistry where it exists. • Consider E/Z stereochemistry of alkenes. • In cases where there is more than one answer, just draw one. • Use R1 to represent coenzyme A and acyl carrier protein. The R group tool is located in the charges and lone pairs drop-down menu.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 dehydration of citrate to yield cis-aconitate, a step in the citric acid cycle, involves the pro-R “arm’’ of citrate rather than the pro-S arm. Which of the following two products is formed?arrow_forward
- Step 7 of the citric acid cycle is shown. Which statement best describes what occurs in this step? CO₂ 1 CH || CH + H₂O CO₂ fumarate CO₂™ fumarase HO C-H CH₂ CO₂ malate A) Fumarate undergoes hydrogenation with hydrogens and electrons provided by the enzyme fumarase. B) Fumarate undergoes hydration with the aid of the enzyme fumarase. C) Fumarate undergoes hydrolysis with the aid of the enzyme fumarase. D) Fumarate undergoes reduction with the aid of the cofactor fumarase.arrow_forwardThe same E1–E2–E3 multienzyme structure found in the pyruvate dehydrogenase and the a-ketoglutarate dehydrogenase complexes is also used in the branched-chain a-ketoacid dehydrogenase complex, which participates in the catabolism of branched-chain amino acids. Draw the reaction product when the following substrate is acted on by the branched-chain a-keto acid dehydrogenase complex.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_forward
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