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Title: In vitro properties of a recombinant flavonol synthase from Arabidopsis thaliana. Author: Prescott AG, Stamford NP, Wheeler G, Firmin JL. Journal: Phytochemistry; 2002 Jul; 60(6):589-93. PubMed ID: 12126705. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]