Abstract
Abstract Melilotate hydroxylase partially purified from extracts of Arthrobacter species catalyzes the stoichiometric conversion of melilotic acid to 2,3-dihydroxyphenylpropionic acid. The hydroxylation is shown to require both reduced nicotinamide adenine dinucleotide and atmospheric oxygen. A partial resolution of the enzyme is achieved with ammonium sulfate. The preparation so treated is almost deviod of enzyme activity, but activity can be completely restored with flavin adenine dinucleotide. The role of melilotate hydroxylase in the general metabolism of coumarin is discussed.
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