Concept explainers
The phosphorylation of
Is this reaction exergonic or endergonic?
How would the value of
Use the value for the hydrolysis of ATP to ADP (Section 27.5) to calculate
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Chapter 27 Solutions
CAREY: ORGANIC CHEMISTRY
- Determine the direction that each of the reactions will progress. Assume that the reactants and products are present in equimolar amounts. The standard free energy of hydrolysis of ATP is –30.5 kJ/mol. fructose+ATP ____fructose 6‑phosphate+ADP The standard free energy of hydrolysis for fructose 6‑phosphate is −15.9 kJ/mol. 3‑phosphoglycerate+ATP___1,3‑bisphosphoglycerate+ADP The standard free energy of hydrolysis for 1,3‑bisphosphoglycerate is −49.3 kJ/mol. creatine+ATP___creatine phosphate+ADP The standard free energy of hydrolysis for creatine phosphate is –43.0 kJ/mol.arrow_forwardFor a given acid HA, it was determined that at pH 6.0 the concentration of the conjugate base [A] was 0.075 M and the acid [HA] was 0.025 M. What percent of this acid is ionized at pH 6.0? What is the pKa of this acid? What pH would this acid be 50% lonized?arrow_forwardThe number of ATP molecules consumed and produced during glycolysis under anaerobic conditions are summarized in the following diagram (the ATP hydrolysis and synthesis reactions are shown in green). Phosphate Carbon atom 2 ATP 2 ADP ●●●●●● Glucose I Energy-Investing Phase O 2 ATP O 6 ATP O 1 ATP 8 ATP NADH + NAD* +H* O 4 ATP ●●●● 2 ADP 2 ATP NADH + NAD +H Based on the diagram above, for each glucose molecule broken down, what is the net energy yield of glycolysis in terms of ATP under anaerobic conditions? Pyruvate 2 ADP 2 ATP ●●●●● Energy-Generating Phase Pyruvatearrow_forward
- Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 °C (310 K). AG' for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7. [malate] = 1.25 mM [oxaloacetate] = 0.130 mM [NAD+] = 440 mM [NADH] = = 180 mM kJ.mol-¹ AG: X10 TOOLSarrow_forwardIntracellular concentrations in resting muscle are as follows: fructose- 6-phosphate, 1.0 mM; fructose-1,6-bisphosphate, 10 mM; AMP, 0.1 mM; ADP, 0.5 mM; ATP, 5 mM; and Pi, 10 mM. Is the phosphofructokinase reaction in muscle more or less exergonic than under standard conditions? By how much?arrow_forwardIf Glutamate + NH4 --> glutamine Delta G = 14.2 kj/mol and ATP + H2O --> ADP + Pi Delta G = -30.5 kj/mol What is true? - overall reaction is non-spontaneous -reaction 2 is non-spontaneous - overall reaction is spontaneous -reaction 1 is spontaneous.arrow_forward
- Chemistry Calculate the standard free-energy for creatine-phosphate hydrolysis in a cell where: creatine-P = 60mmol, creatine = 30 mmol, ATP = 1 mmol, ADP = 0.1 mmol. Is this reaction exer/endergonic?arrow_forwardWhen the following reaction reached equilibrium the concentration of glucose 1-phosphate is 34mM, and the concentration of glucose 6-phosphate is 190mM. At standard temperatures and pressure, calculate the Keq and the ΔGo' glucose 6-phosphate <---(phosphoglucoisomerase)---> glucose 1-phosphate Keq= ΔGo' =arrow_forwardA solution of the enzyme glycogen synthase incubated at 45°C lost 70% of its activity in 3 minutes „but when incubated at 45°C in the presence of a very large concentration of its substrate UDP- Glucose, it lost only 3% of its activity in the same amount of time, Why? Clu CH,OH CH, OH HO, он CH;OH CH2OH но HO он HO UDP O-P-0 OH OH NH o--o CH, OH CH2OH CH,OH OH OH HO UDP-glucose binding makes it easier for the enzyme to unfold. The enzyme likely had phosphate groups added through covalent modification. O Interactions with the bound UDP-glucose stabilize the tertiary structure of glycogen synthase. The UDP-Glucose is a positíve effector which increases the enzyme activity.arrow_forward
- The hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 umol of pyrophosphate in 15 minutes. The purified enzyme has a Vnax of 2800 U per milligram of enzyme. When (S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second? Vnax = umol -s. mg- If cach enzyme subunit has one active site, how many micromoles of active sites, or (E]r, are there in 1 mg of enzyme? (Er = umol - mg-arrow_forwardQ2 CH,OH CH,OPO,2- H H OH H OH 0-PO,2- но но OH H. OH OH Glucose-1-phosphate Glucose-6-phosphate Calculate the standard free-energy change (AG°) fo the reaction catalyzed by the enzyme phosphoglucomutase. When at standard temperature (25 °C) and pressure, the equilibrium of each molecule is 1 mM glucose 1-phosphate and 19 mM glucose 6-phosphate. HINT: at 25 °C, RT = 2.479 kJ/molarrow_forwardAnswer True or False The Na/K-ATPase pump is an example of a coupling element between a spontaneous process and a non spontaneous process.arrow_forward
- General Chemistry - Standalone book (MindTap Cour...ChemistryISBN:9781305580343Author:Steven D. Gammon, Ebbing, Darrell Ebbing, Steven D., Darrell; Gammon, Darrell Ebbing; Steven D. Gammon, Darrell D.; Gammon, Ebbing; Steven D. Gammon; DarrellPublisher:Cengage LearningChemistry & 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 Learning
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