Abstract
An enzyme cinnabarinic acid synthase which catalyzes the oxidative dimerization of 2 moles of 3-hydroxyanthranilic acid to 1 mole of cinnabarinic acid has been partially purified from the leaves of Tecoma stans. The enzyme showed an absolute requirement for Mn++ ions. The optimum pH was around 8.0 and optimum temperature was 30°. The Km value is 3.6 × 10−4 M. Several divalent metal ions as well as metal chelating agents inhibited the reaction. The enzyme activity was highly susceptible to a variety of reducing agents. Sulphydryl inhibitors did not inhibit the reaction. Electron acceptors had no effect on enzyme activity, though cytochrome c slightly activated the reaction. Cytochrome c reduced by 3-hydroxyanthranilic acid was reoxidized by the enzyme preparation. The system was specific for 3-hydroxyanthranilic acid and cytochrome c reduced by o-aminophenol or ascorbic acid was not reoxidized.
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