A flavoprotein (FAD) with high specificity for monoprenyl isoflavone. The product of the prenyl epoxidation reaction contains an oxygen atom derived from O2, but not from H2O. It is slowly and non-enzymically converted into the corresponding dihydrofurano derivative. The enzyme in the fungus Botrytis cinerea is induced by the substrate analogue, 6-prenylnaringenin.
EC 18.104.22.168 created 2000
Tanaka, M. and Tahara, S.
FAD-dependent epoxidase as a key enzyme in fungal metabolism of prenylated flavonoids.