1. In vitro properties of a recombinant flavonol synthase from Arabidopsis thaliana.
- Author
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Prescott AG, Stamford NP, Wheeler G, and Firmin JL
- Subjects
- Catalysis, Escherichia coli genetics, Escherichia coli metabolism, Molecular Conformation, Oxidoreductases genetics, Recombinant Proteins genetics, Recombinant Proteins metabolism, Arabidopsis enzymology, Flavanones, Flavonoids metabolism, Oxidoreductases metabolism, Plant Proteins, Quercetin analogs & derivatives, Quercetin metabolism
- 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.
- Published
- 2002
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