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.
John Innes Centre, Norwich NR4 7UH, UK.
Andrea G
AG
Prescott
Nicholas P J
NP
Stamford
Guy
G
Wheeler
John L
JL
Firmin
D017360:Arabidopsis / Q000201:enzymology*; D002384:Catalysis; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D044950:Flavanones; D005419:Flavonoids / Q000378:metabolism*; D008968:Molecular Conformation; D010088:Oxidoreductases / Q000235:genetics / Q000378:metabolism*; D010940:Plant Proteins; D011794:Quercetin / Q000031:analogs & derivatives* / Q000378:metabolism*; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
D044950:Flavanones; D005419:Flavonoids; D010940:Plant Proteins; D011994:Recombinant Proteins; C080220:aromadedrin; D011794:Quercetin; D010088:Oxidoreductases; C085313:flavonol synthase; C005273:naringenin