Abstract
Abstract Enzyme preparations from flowers of defined genotypes of Matthiola incana contain two dif ferent hydroxylases for hydroxylation of naringenin in the 3-and 3′-position, respectively. The 3-hydroxylase is a soluble enzyme and requires as cofactors 2-oxoglutarate, Fe2+ and ascorbate. Besides naringenin eriodictyol is a substrate for the 3-hydroxylase. The 3′-hydroxylase is localized in the microsomal fraction and requires NADPH as cofactor. Naringenin and dihydro-kaempferol but not 4-coumarate or 4-coumaroyl-CoA are substrates for this enzyme. 3′-Hydroxylase activity is present only in genetic lines of M. incana with the wild-type allele b+.
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