(a)
Interpretation:
The standard energy change for the phosphoglycerate reaction should be calculated
Concept Introduction:
The energy which allows predicting the reaction spontaneously at a particular temperature is called free energy. The reaction which proceed both forward and backward reaction is called as equilibrium constant K.
Answer to Problem 15P
Explanation of Solution
In phosphoglycerate reaction ATP combine with hydrolysis to obtain following equation.
In the first reaction hydrolysis of 1,3-BPG mixes to give
In the second reaction, it is reverse process of hydrolysis of ATP. In this reaction we use opposite value of free energy.
In the coupled reaction free energy stated as
In phosphoglycereate kinase reaction the standard free energy obtained is
(b)
Interpretation:
The equilibrium constant of the reaction should be calculated.
Concept Introduction:
The energy which allows predicting the reaction spontaneously at a particular temperature is called free energy. The reaction which proceed both forward and backward reaction is called as equilibrium constant K
Answer to Problem 15P
Explanation of Solution
Hence
The temperature of the body is
Convert Celsius to Kelvin
Substitute the equation in following formula.
The equilibrium constant for the reaction is
(c)
Interpretation:
The ratio of
Concept Introduction:
The energy which allows predicting the reaction spontaneously at a temperature is called free energy. The reaction which proceed both forward and backward reaction is called as equilibrium constant K
Answer to Problem 15P
Explanation of Solution
The steady state concentration for the reaction is
Concentration ratio for
Substitute the value
Rearrange the equation to get ratio of ATP AND ADP
The ratio of
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Chapter 18 Solutions
Biochemistry
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- АCTIVITY 5.1.1 Determine the catalytic power of jack bean urease in catalyzing the hydrolysis of urea given the following conditions: At 200, the rate constant for enzyme-catalyzed reaction is 3x104/sec The rate constant for the uncatalyzed hydrolysis of urea is 3x10-10/sec.arrow_forwardActivity of pesin in the blood at pH 7.4arrow_forward1. pH Effects a. In the enzyme mechanism of lysozyme, two acidic amino acid residues, Asp52 and Glu35, are critical for catalytic activity. If we assume normal side chain pKa values for Asp (pKar = 3.90) and for Glu (pKar = 4.07), what proportion of enzyme molecules will have both Asp52 and Glu35 in the correct ionization state at pH 5.0 (the pH optimum for lysozyme)? b. Are the traditional pKa values likely to be correct within the protein? What pKa changes might be present within lysozyme?arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning