In vitro properties of a recombinant flavonol synthase from Arabidopsis thaliana

被引：147

作者：

Prescott, AG

Stamford, NPJ ^{[1
]}

Wheeler, G

Firmin, JL

机构：

[1] Univ E Anglia, Sch Chem Sci, Norwich NR4 7TJ, Norfolk, England

[2] John Innes Ctr, Norwich NR4 7UH, Norfolk, England

来源：

PHYTOCHEMISTRY | 2002年 / 60卷 / 06期

基金：

英国生物技术与生命科学研究理事会;

关键词：

Arabidopsis thaliana; Brassicaceae; flavonoid biosynthesis; flavonol synthase; 2-oxoglutarate-dependent dioxygenase; recombinant enzyme;

D O I：

10.1016/S0031-9422(02)00155-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：589 / 593

页数：5

共 22 条

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Novel flavonol 2-oxoglutarate dependent dioxygenase: Affinity purification, characterization, and kinetic properties [J].