Concept explainers
A student is trying to determine the mechanism for a reaction that uses ATP to activate a carboxylate ion, which then reacts with a thiol. If the carboxylate ion attacks the γ-phosphorus of ATP, the reaction products are the thioester, ADP, and phosphate. However, whether it attacks the α-phosphorus or the β-phosphorus of ATP cannot be determined from the reaction products because the thioester, AMP, and pyrophosphate would be the products in both reactions. The mechanisms can be distinguished by a labeling experiment in which the enzyme, the carboxylate ion, ATP, and radioactively labeled pyrophosphate are incubated, and ATP is isolated. If the isolated ATP is radioactive, attack occurred on the α-phosphorus. If it is not radioactive, then attack occurred on the β-phosphorus. Explain these conclusions.
Want to see the full answer?
Check out a sample textbook solutionChapter 19 Solutions
Essential Organic Chemistry, Global Edition
- 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_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
- The enzyme that catalyzes reaction below can be classified as: NAD* NADH + H* Но- H-Ć- Н—с—н H- malate dehydrogenase Oxaloacetate Malatearrow_forwardAdenylyl cyclase catalyzes the conversion of ATP to cyclic AMP (CAMP). This reaction occurs via a nucleophilic substitution. Label the atoms that act as the nucleophile and the electrophile in the cyclization of ATP to CAMP. H,N. nucleophile HO-P-0- он OH OH OH он electrophilearrow_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_forward
- Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout, several medications are used to inhibit the activity of xanthine oxidase and reduce the production of uric acid. You are a biochemist and just discovered a chemical that can inhibit the activity of the human xanthine oxidase. When analyzing its mode of inhibition, you found that the enzyme inhibitor complex requires 450 J.mol-1 to dissociate and that it displays kinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministry of health for approval as a medication for gout. Based on the data provided, are they going to authorize it as a medication or not? Explain?arrow_forwardIn this section of the course, you have come across two drugs which inhibit dihydrofolate reductase. One of thes drugs is used as an antibacterial drug and the other is used in treatment of cancer. Why is it that each of these drugs can only be used for one purpose (and not the other) in clinical medicine.arrow_forwardMalate is converted to oxaloacetate by the enzyme malate dehydrogenase in the final reaction of the citrate cycle. This redox reaction results in the reduction of NAD+ to generate NADH + H+. Answer the three questions below and choose the correct answer. (a) Calculate the delta AE for the malate dehydrogenase reaction. (b) Calculate AG and determine if the conversion from malate to oxaloacetate is favorable under standard biochemical conditions using the information below. (c) Under cellular conditions is the AG favorable or unfavorable? Oxaloacetate + 2H* + 2e- --> Malate E° = -0.17 V NAD* + H+ + 2e- --> NADH E°' = -0.32 Varrow_forward
- Draw the complete, step-wise mechanism of a phosphate transfer reaction that follows a concerted pathway or SN2 type reaction pathway. Clearly depict the transition state of the reaction.. R₁ B: ti R2 ertarrow_forwardNeostigmine is an inhibitor of acetylcholinesterase. The enzyme attempts to catalyse the same reaction on neostigmine as it does with acetylcholine. However, a stable intermediate is formed which prevents completion of the process and which results in a molecule being covalently linked to the active site. Identify (draw) the stable intermediate and explain why it is stable.arrow_forwardThe enzyme that catalyzes this reaction is a(n) H 1000 CH3 Acetaldehyde Otransferase NADH + H+ ligase Olyase oxidoreductase hydrolase alcohol dehydrogenase NAD+ OH CH2 CH3 Ethanolarrow_forward
- Organic ChemistryChemistryISBN:9781305580350Author:William H. Brown, Brent L. Iverson, Eric Anslyn, Christopher S. FootePublisher:Cengage Learning
- Chemistry & Chemical ReactivityChemistryISBN:9781337399074Author:John C. Kotz, Paul M. Treichel, John Townsend, David TreichelPublisher:Cengage LearningChemistry & Chemical ReactivityChemistryISBN:9781133949640Author:John C. Kotz, Paul M. Treichel, John Townsend, David TreichelPublisher:Cengage LearningGeneral, Organic, and Biological ChemistryChemistryISBN:9781285853918Author:H. Stephen StokerPublisher:Cengage Learning