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.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Arabidopsis / enzymology*
-
Catalysis
-
Escherichia coli / genetics
-
Escherichia coli / metabolism
-
Flavanones*
-
Flavonoids / metabolism*
-
Molecular Conformation
-
Oxidoreductases / genetics
-
Oxidoreductases / metabolism*
-
Plant Proteins*
-
Quercetin / analogs & derivatives*
-
Quercetin / metabolism*
-
Recombinant Proteins / genetics
-
Recombinant Proteins / metabolism
Substances
-
Flavanones
-
Flavonoids
-
Plant Proteins
-
Recombinant Proteins
-
aromadedrin
-
Quercetin
-
Oxidoreductases
-
flavonol synthase
-
naringenin