1. Calculation of AG from an Equilibrium Constant Calculate the standard free-energy change for eachof the following metabolically important enzyme-catalyzed reactions, using the equilibrium constants givenfor the reactions at 25 °C and pH 7.0, R = 8.315 J/molKAspartate aminotranterase(a)Glutamate + oxaloacetate 2 aspartate + a-ketoglutarate Keg-6.8Triosephosphate isomerase(b)Dihydroxvacetonephosphate glyceraldehyde3phosphate Keg-0.0475phosphofructokinasee fructose1,6-bisphosphate+ADP Keg=254(c)Fructose6-phosphate + ATP

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1. Calculation of AG from an Equilibrium Constant Calculate the standard free-energy change for each of the following metabolically important enzyme-catalyzed reactions, using the equilibrium constants given for the reactions at 25 °C and pH 7.0, R = 8.315 J/mol K Aspartate amingtranferase (a)Glutamate + oxaloacetate 2 aspartate +a-ketoglutarate Keg-6.8 Triosephosphate isomerase (b)Dihydroxvacetonephosphate glyceraldehyde3phosphate Keg-0.0475 phosphofructokinase + ATP = fructose1,6-bisphosphate+ADP Keg-254 (c)Fructose6-phosphate

1. Calculation of AG from an Equilibrium Constant Calculate the standard free-energy change for each of the following metabolically important enzyme-catalyzed reactions, using the equilibrium constants given for the reactions at 25 °C and pH 7.0, R = 8.315 J/mol K Aspartate amingtranferase (a)Glutamate + oxaloacetate 2 aspartate +a-ketoglutarate Keg-6.8 Triosephosphate isomerase (b)Dihydroxvacetonephosphate glyceraldehyde3phosphate Keg-0.0475 phosphofructokinase + ATP = fructose1,6-bisphosphate+ADP Keg-254 (c)Fructose6-phosphate

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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