Abstract
The exchange of bound FAD for free FAD was studied with D-amino acid oxidase (D-amino acid:oxygen oxidoreductase (deaminating), EC 1.4.3.3) and β- d-glucose oxidase (β- d-glucose:oxygen 1-oxidoreductase, EC 1.1.3.4). For a simple measurement of the reaction rate, equimolar amounts of the enzyme and [ 14C]FAD were mixed. The exchange occurred very rapidly in the holoenzyme of d-amino acid oxidase at 25°C, ph 8.3 (half life of the exchange: 0.8 min), but slowly in the presence of the substrate or a competitive inhibitor, benzoate. It also occurred slowly in the purple complex of d-amino acid oxidase. In the case of β- d-glucose oxidase, however, the exchange occurred very slowly at 25°C, ph 5.6, regardless of the presence of the substrate or p-chloromercuribenzoate. On the basis of these findings, the turnover of the coenzymes of flavin enzymes in mammals is discussed.
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