Biochemistry: Concepts and Connections (2nd Edition)
Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 16, Problem 2P

If palmitic acid is subjected to complete combustion in a bomb calorimeter, one can calculate a standard free energy of combustion of 9788 kJ/moI. From the ATP yield of palmitate oxidation, what is the metabolic efficiency of the biological oxidation, in terms of kilojoules saved as ATP per kilojoule released? (Ignore the cost of fatty acid activation.)

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For a Michaelis-Menten reaction, k₁-5 x 10'/M-s, k.-2 x 10%/s, and k₂-4 x 10²/s. a) Calculate the Ks and KM for this reaction. b) Does substrate binding achieve equilibrium or steady state?
Assume that an enzyme-catalyzed reaction follows the scheme shown: E+S SES →E + P k₁ = 1 x 109/M-s k-1=2.5 x 10%/s k₂ = 3.4 x 107/s What is the dissociation constant for the enzyme-substrate, K,? What is the Michaelis constant, Km, for this enzyme? What is the turnover number, Keat, for this enzyme? What is the catalytic efficiency for the enzyme? If the initial Et concentration is 0.25mM, what is Vmax?
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