The apparent Michaelis constants of each component for the coenzyme are the same values. Each component is inhibited by the substrate according to the same mechanism. The optimal pH values and the equilibrium constants of the reactions catalyzed by each component are the same. E1%1cm (280mμ) values of each component are are identical. E280mμ/E260mμ absorption ratios also similar. It may be concluded that each component is almost the same enzyme protein.
