Concept explainers
Interpretation:
The reaction obtained by coupling hydrolysis of
Concept Introduction:
Exergonic: The reaction is considered as exergonic if energy released since the reactants loses its energy making the free energy more negative hence making it spontaneous reaction.
Endergonic: The reaction is considered as endergonic if it needs more energy means that activation energy is much higher making the reaction non spontaneous.
Favorable Reaction: They release free energy which in turn used to do work. The products will have lower energy than reactants of the reaction shows that stable products are obtained hence the value of
The tendency for reaction proceed toward product side before reaching equilibrium will increases as more amount of free energy released.
Hydrolysis: The reaction in which chemical compound is breakdown in presence of water is termed as hydrolysis. Here water serves as one reactant.
Phosphorylation: It involves transfer of phosphate group from inorganic/organic phosphate to another chemical compound.
Want to see the full answer?
Check out a sample textbook solutionChapter 21 Solutions
Fundamentals Of General, Organic And Biological Chemistry In Si Units
- The conversion of dihyroxyacetone phosphate to glyceraldehyde 3-phosphate, catalyzed by triose phosphate isomerase, has an equilibrium constant of Keq’ = 0.0475. Calculate the standard free-energy change for this reaction at 25ºC and pH 7.0.arrow_forwardIn a major metabolic pathway involving the monosaccharide glucose, one of the reactions involve the conversion of glucose to glucose-6-phosphate summarized below together with accompanying free energy change: glucose + phosphate glucose-6-phosphate + H,0 AG = 13.8 kJ · mol-1 (Reaction 1) Is the reaction to produce glucose-6-phosphate (usually abbreviated as G6P) a favorable (i.e. spontaneous) one? Explain.arrow_forwardThe enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose 6-phosphate. After the reactants and products were mixed and allowed to reach equilibrium at 25°C, the concentration of glucose 1-phosphate was 4.5 mM and that of glucose 6-phosphate was 86 mM. Calculate Keq' and AG for this reaction. The reaction coordinate diagram for an enzyme-catalyzed reaction is shown below. How many transition states and intermediates are in the reaction? Is the reaction thermodynamically favorable? Which step is the rate-determining step of the reaction? G Reaction coordinatearrow_forward
- A table of standard state free energies is shown below. For the reaction: Creatine phosphate + ADP----> Creatine + ATP the free energy under standard state conditions is kJ/mole. TABLE 14.1 Standard free energies of hydrolysis of some phosphorylated compounds Compound kcal mol kJ mol - 14.8 Phosphoenolpyruvate 1,3-Bisphosphoglycerate Creatine phosphate ATP (to ADP) Glucose 1-phosphate Pyrophosphate Glucose 6-phosphate -61.9 -11.8 - 49.4 - 10.3 -43.1 - 7.3 - 30.5 - 20.9 - 19.3 - 5.0 - 4.6 – 3.3 -13.8 Glycerol 3-phosphate – 2.2 - 9.2 A. +12.6 В. +73.6 С.-3.0 D. -12.6 ОЕ.-73.6arrow_forwardLithium ion inhibits the synthesis of inositol trisphosphate by inhibiting a reaction in the breakdown of inositol trisphosphate. Explain this apparent paradox.arrow_forwardLithium ion inhibits the synthesis of inositol trisphosphate by inhibiting a reaction in the breakdown of inositol trisphosphate.Explain this apparent paradox.arrow_forward
- In the degradation of glycogen, the purpose of the debranching enzyme is to remove the last four glucose molecules from branches structure of glycogen. It does this by catalyzing three different reactions. Use the equations below to answer parts a-c. Synthesis of α(1,6) link ΔG = +7.1 kJ Hydrolysis of α(1,4) link ΔG = ─15.5 kJ a)What are the three chemical reactions performed during the removal of the last four glucose molecules of the branching structure of glycogen? b) Calculate ΔG for each of the three reactions described in part a. c) Now calculate the overall energy change for the net reaction carried out by this enzyme. d) Why is this reaction favorable?arrow_forwardThe plant toxin fluoroacetate (F-CH2COO−) is easily converted to fluorocitrate when an animal ingests the plant. The enzyme aconitase has a high affinity for the 2-fluorocitrate molecule. Consider the purpose of this enzyme and speculate as to why the reaction to produce isocitrate does not occur as planned. Why is fluoroacetate considered a poison? [Hint: Fluorine is more electronegative than oxygen.]arrow_forwardThe standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1 kJ/mol. Calculate the equilibrium constant for the reaction. Calculate AG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM. Is the reaction spontaneous under these conditions? HOCH, -20;POCH, H H H H H H ОН Н НО ОН Н H НО ОН H ОН H. ОН Glucose-l-phosphate Glucose-6-phosphatearrow_forward
- Write the coupled reaction that would occur spontaneously for the following pairs of molecules under standard condition: Oxaloaxcetate and NAD+arrow_forwardThe standard Gibbs (free) energy of reaction (A,Gº') of the following reaction is equal to zero (at 25 °C and pH 7) pyruvate + aspartate Pyruvate, aspartate and L-alanine are mixed each at a concentration of 1 mM, without oxaloacetate. Calculate the molar concentrations of each compound when the reaction reaches equilibrium. oxaloacétate + L-alaninearrow_forwardAn L-amino acid oxidase in mammalian peroxisomes requires H2O and O2 as substrates and catalyzes amino acid deamination, producing H2O2 as a product. Write a balanced equation for the reaction.arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON