Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
8th Edition
ISBN: 9780134015187
Author: John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
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Textbook Question
Chapter 25, Problem 25.35AP
How do essential and nonessential amino acids differ from each other in the number of steps required for their synthesis in organisms that synthesize both?
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Chapter 25 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
Ch. 25.2 - Prob. 25.1PCh. 25.2 - Prob. 25.2KCPCh. 25.3 - Prob. 25.3PCh. 25.3 - Prob. 25.4PCh. 25.3 - Prob. 25.5PCh. 25.3 - Prob. 25.6PCh. 25.4 - Prob. 25.1CIAPCh. 25.4 - Prob. 25.2CIAPCh. 25.4 - Prob. 25.3CIAPCh. 25.4 - Prob. 25.7P
Ch. 25.4 - Prob. 25.8KCPCh. 25.6 - Prob. 25.9PCh. 25.6 - Prob. 25.10KCPCh. 25.6 - What is meant by a conditional amino acid?Ch. 25.6 - Prob. 25.5CIAPCh. 25.6 - Prob. 25.6CIAPCh. 25 - In the diagram shown here, fill in the sources for...Ch. 25 - Prob. 25.12UKCCh. 25 - Prob. 25.13UKCCh. 25 - Prob. 25.14UKCCh. 25 - Prob. 25.15UKCCh. 25 - Prob. 25.16UKCCh. 25 - Prob. 25.17APCh. 25 - Prob. 25.18APCh. 25 - Prob. 25.19APCh. 25 - Prob. 25.20APCh. 25 - Prob. 25.21APCh. 25 - Prob. 25.22APCh. 25 - What is the structure of the -keto acid formed...Ch. 25 - Prob. 25.24APCh. 25 - In general, how does oxidative deamination differ...Ch. 25 - Prob. 25.26APCh. 25 - Prob. 25.27APCh. 25 - Prob. 25.28APCh. 25 - Prob. 25.29APCh. 25 - Prob. 25.30APCh. 25 - Prob. 25.31APCh. 25 - Prob. 25.32APCh. 25 - Prob. 25.33APCh. 25 - Prob. 25.34APCh. 25 - How do essential and nonessential amino acids...Ch. 25 - Prob. 25.36APCh. 25 - Prob. 25.37APCh. 25 - How is tyrosine biosynthesized in the body? What...Ch. 25 - Prob. 25.39APCh. 25 - Prob. 25.40APCh. 25 - Prob. 25.41APCh. 25 - What energy source is used in the formation of...Ch. 25 - Write the equation for the transamination reaction...Ch. 25 - Prob. 25.44CPCh. 25 - Prob. 25.45CPCh. 25 - Prob. 25.46CPCh. 25 - Prob. 25.47CPCh. 25 - Prob. 25.48CPCh. 25 - Prob. 25.49CPCh. 25 - Prob. 25.50CPCh. 25 - Prob. 25.51CPCh. 25 - Prob. 25.52CPCh. 25 - Why might it be a bad idea to take large...Ch. 25 - Prob. 25.54GPCh. 25 - Prob. 25.55GPCh. 25 - Prob. 25.56GP
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- After adding a small amount of ATP labeled with radioactive phosphorus in the terminal position, [7-32P]ATP, to a yeast extract, a researcher finds about half of the 32P activity in P; within a few minutes, but the concentration of ATP remains unchanged. She then carries out the same experiment using ATP labeled with 32P in the central position, [ẞ-³2P]ATP, but the 32P does not appear in P; within such a short time. Which statements explain these results? Yeast cells reincorporate P; released from [ß-³2P]ATP into ATP more quickly than P¡ released from [y-³2P]ATP. Only the terminal (y) phosphorous atom acts as an electrophilic target for nucleophilic attack. The terminal (y) phosphoryl group undergoes a more rapid turnover than the central (B) phosphate group. Yeast cells maintain ATP levels by regulating the synthesis and breakdown of ATP. Correct Answerarrow_forwardCompare the structure of the nucleoside triphosphate CTP with the structure of ATP. NH₂ 0- 0- 0- ·P—O—P—O—P—O—CH₂ H H H H OH OH Cytidine triphosphate (CTP) Consider the reaction: ATP + CDP ADP + CTP NH 0- 0- 0- ¯0— P—O— P—O—P-O-CH₂ H Η о H H OH OH Adenosine triphosphate (ATP) NH₂ Now predict the approximate K'eq for this reaction. Now predict the approximate AG for this reaction. Narrow_forwardThe standard free energy, AGO, of hydrolysis of inorganic polyphosphate, polyP, is about −20 kJ/mol for each P; released. In a cell, it takes about 50 kJ/mol of energy to synthesize ATP from ADP and Pi. ○ P O Inorganic polyphosphate (polyP) Is it feasible for a cell to use polyP to synthesize ATP from ADP? Why or why not? No. The reaction is unidirectional and always proceeds in the direction of polyP synthesis from ATP. Yes. If [ADP] and [polyP] are kept high, and [ATP] is kept low, the actual free-energy change would be negative. No. The synthesis of ATP from ADP and P; has a large positive G'o compared to polyP hydrolysis. Yes. The hydrolysis of polyP has a sufficiently negative AG to overcome the positive AGO of ATP synthesis. Correct Answerarrow_forward
- In 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 to fructose 6-phosphate (as shown in the diagram) occurs two steps before the cleavage reaction. The intervening step is phosphorylation of fructose 6-phosphate to fructose 1,6-bisphosphate. H H | H-C-OH H-C-OH C=0 HO-C-H HO-C-H phosphohexose isomerase H-C-OH H-C-OH H-C-OH H-C-OH CH₂OPO CH₂OPO Glucose 6-phosphate Fructose 6-phosphate What does the isomerization step accomplish from a chemical perspective? Isomerization alters the molecular formula of the compound, allowing for subsequent phosphorylation. Isomerization moves the carbonyl group, setting up a cleavage between the central carbons. Isomerization causes the gain of electrons, allowing for the eventual release of NADH. Isomerization reactions cause the direct production of energy in the form of ATP.arrow_forwardFrom data in the table, calculate the AG value for the reactions. Reaction AG' (kJ/mol) Phosphocreatine + H₂O →>> creatine + P -43.0 ADP + Pi → ATP + H₂O +30.5 Fructose +P → fructose 6-phosphate + H₂O +15.9 Phosphocreatine + ADP creatine + ATP AG'O ATP + fructose → ADP + fructose 6-phosphate AG'° kJ/mol kJ/molarrow_forwardMacmillan Learning The phosphorylation of glucose to glucose 6-phosphate is the initial step in the catabolism of glucose. The direct phosphorylation of glucose by P, is described by the equation Glucose + P ← glucose 6-phosphate + H₂O AG = 13.8 kJ/mol Coupling ATP hydrolysis to glucose phosphorylation makes thermodynamic sense, but consider how the coupling might take place. Given that coupling requires a common intermediate, one conceivable mechanism is to use ATP hydrolysis to raise the intracellular concentration of Pi. The increase in P; concentration would drive the unfavorable phosphorylation of glucose by Pi- Is increasing the P; concentration a reasonable way to couple ATP hydrolysis and glucose phosphorylation? No. The phosphate salts of divalent cations would be present in excess and precipitate out. Yes. Increasing the concentration of P; would decrease K'eq and shift equilibrium to the right. Yes. The extra ATP hydrolysis would provide enough free energy to drive the…arrow_forward
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