The hydration of CO2is catalyzed by the enzyme carbonic anhydrase. The steady-state kineti...

The hydration of CO2

is catalyzed by the enzyme carbonic anhydrase. The steady-state kinetics of the forward (hydration) and reverse (dehydration) reactions at pH 7.1, 0.5°C, and 2 mM phosphate buffer was studied using bovine carbonic anhydrase (H. DeVoe and G. B. Kistiakowsky, 1961, J. Am. Chem. Soc. 83:274). Some typical results for an enzyme concentration of 2.3 nM are

Plot the data in an appropriate way and determine the Michaelis constant KM and the rate coefficient k2 for the decomposition of the enzyme-substrate complex to form product for

a. The hydration reaction.

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b. The dehydration reaction.

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c. From your results, calculate the equilibrium constant for the reaction

(Hint: Start by writing an equation that defines the equilibrium condition in terms of the Michaelis-Menten formulation of this reaction. Note that the kinetics was measured at pH 7.1.)