In vitro properties of a recombinant flavonol synthase from Arabidopsis thaliana

cDNA corresponding to a flavonol synthase gene from Arabidopsis thaliana was cloned and expressed in Escherichia coli. The recombinant protein was purified to near-homogeneity and the catalytic properties of the enzyme were studied in vitro. Together with kaempferol and apigenin the recombinant protein synthesised the (2R,3S)-cis- and (2S,3S)-trans-isomers of dihydrokaempferol from the (2S)- and (2R)-isomers of naringenin, respectively. Flavanones and dihydroflavanols differing in degree of A- or B-ring hydroxylation were also accepted as substrates.