Apigenin produced by maize flavone synthase I and II protects plants against UV-B-induced damage

2018 ◽  
Vol 42 (2) ◽  
pp. 495-508 ◽  
Author(s):  
Silvana Righini ◽  
Eduardo José Rodriguez ◽  
Carla Berosich ◽  
Erich Grotewold ◽  
Paula Casati ◽  
...  
Keyword(s):  
Flavone Synthase

Expression of a soluble flavone synthase allows the biosynthesis of phytoestrogen derivatives in Escherichia coli

2006 ◽  
Vol 70 (1) ◽  
pp. 85-91 ◽  
Author(s):  
Effendi Leonard ◽  
Joseph Chemler ◽  
Kok Hong Lim ◽  
Mattheos A. G. Koffas
Keyword(s):  
Escherichia Coli ◽  
Flavone Synthase

Molecular and biochemical characterization of torenia flavonoid 3′-hydroxylase and flavone synthase II and modification of flower color by modulating the expression of these genes

Plant Science ◽  
2002 ◽  
Vol 163 (2) ◽  
pp. 253-263 ◽  
Author(s):  
Yukiko Ueyama ◽  
Ken-ichi Suzuki ◽  
Masako Fukuchi-Mizutani ◽  
Yuko Fukui ◽  
Kiyoshi Miyazaki ◽  
...  
Keyword(s):  
Biochemical Characterization ◽  
Flower Color ◽  
Flavone Synthase ◽  
Flavone Synthase Ii

Screening and heterologous expression of flavone synthase and flavonol synthase to catalyze hesperetin to diosmetin

2021 ◽  
Vol 43 (11) ◽  
pp. 2161-2183
Author(s):  
Zhen Wang ◽  
Xu Huang ◽  
Juan Liu ◽  
Feiyao Xiao ◽  
Miaomiao Tian ◽  
...  
Keyword(s):  
Heterologous Expression ◽  
Flavonol Synthase ◽  
Flavone Synthase

Enzymatic Synthesis of 4′-and 3′, 4′ -Hydroxylated Flavanones and Flavones with Flower Extracts of Sinningia cardinalis

1987 ◽  
Vol 42 (11-12) ◽  
pp. 1193-1199 ◽  
Author(s):  
K. Stich ◽  
G. Forkmann
Keyword(s):  
Enzymatic Synthesis ◽  
Microsomal Fraction ◽  
Chalcone Synthase ◽  
Condensation Reaction ◽  
Flavonoid Biosynthesis ◽  
Hydroxylase Activity ◽  
Key Enzyme ◽  
Flavone Synthase ◽  
Flavone Synthase Ii ◽  
Cytochrome P 450

Flowers of Sinningia (syn. Rechsteineria) cardinalis contain glycosides of the flavones apigenin (4′-OH) and luteolin (3′,4′-OH) respectively, and of the related 3-deoxyanthocyanidins apigeninidin and luteolinidin. Studies on substrate specificity of the key enzyme of flavonoid biosynthesis, chalcone synthase, revealed that the 3′,4′-hydroxylated flavonoids are formed by hydroxylation of flavonoid compounds rather than by incorporation of caffeoyl-CoA into the flavonoid skeleton during the condensation reaction. In fact, flavonoid 3′-hydroxylase activity could be demonstrat­ed in the microsomal fraction of the flower extracts. The enzyme catalyses hydroxylation of naringenin and apigenin in the 3′-position to eriodictyol and luteolin, respectively, with NADPH as cofactor. Besides flavanone 3′-hydroxylase a further NADPH-dependent enzyme activity (flavone synthase II) was observed in the microsomal fraction catalysing the oxidation of naringenin to apigenin and of eriodictyol to luteolin. The Cytochrome P-450 inhibitor ancymidol was found to abolish completely flavone synthase II activity, whereas flavonoid 3′-hydroxylase activity was not impaired.

scholarly journals Unraveling the Biochemical Base of Dahlia Flower Coloration

2008 ◽  
Vol 3 (8) ◽  
pp. 1934578X0800300 ◽  
Author(s):  
Heidi Halbwirth ◽  
Gerlinde Muster ◽  
Karl Stich
Keyword(s):  
Chalcone Synthase ◽  
Flower Color ◽  
Chalcone Isomerase ◽  
Anthocyanin Content ◽  
Anthocyanin Accumulation ◽  
Enzyme Preparations ◽  
Yellow Color ◽  
Flavone Synthase ◽  
Flavone Synthase Ii ◽  
Related Compounds

Dahlia ( Dahlia variabilis) exists in a dazzling array of cultivars, showing red, orange, magenta, lilac, yellow and white flower color, which is exclusively based on the presence of flavonoids and biochemically related compounds. Red hues (red, orange, magenta, lilac) are a result of anthocyanin accumulation in varying concentration and composition, while a yellow color is based on the formation of 6′-deoxychalcones in the petals. Red dahlia pigments are all derived from pelargonidin and cyanidin. Delphinidin derivatives are not formed due to the absence of flavonoid 3′,5′-hydroxylase in dahlia petals, which provides an explanation for the lack of blue dahlia flowers. Orange, lilac and rose cultivars are characterized by a lower anthocyanin content compared to many red cultivars. We investigated 198 cultivars for the presence of flavonoid enzymes. The activities of chalcone isomerase (CHI), chalcone synthase (CHS), dihydroflavonol 4-reductase (DFR), flavanone 3-hydroxylase (FHT), flavone synthase II (FNSII), flavonol synthase (FLS) and flavonoid 3′-hydroxylase (F3′H) were demonstrated in enzyme preparations of dahlia petals. CHI accepted 6′-hydroxychalcones as substrates, but did not catalyze the conversion of 6′-deoxychalcones to the corresponding flavanones. White cultivars were frequently characterized by the lack of DFR activity, whereas in many yellow cultivars neither FHT nor DFR activity could be shown.

Cloning of parsley flavone synthase I

2001 ◽  
Vol 58 (1) ◽  
pp. 43-46 ◽  
Author(s):  
Stefan Martens ◽  
Gert Forkmann ◽  
Ulrich Matern ◽  
Richard Lukačin
Keyword(s):  
Flavone Synthase

scholarly journals Evolution of Flavone Synthase I from Parsley Flavanone 3β-Hydroxylase by Site-Directed Mutagenesis

2007 ◽  
Vol 144 (3) ◽  
pp. 1442-1454 ◽  
Author(s):  
Yvonne Helen Gebhardt ◽  
Simone Witte ◽  
Holger Steuber ◽  
Ulrich Matern ◽  
Stefan Martens
Keyword(s):  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Flavone Synthase

Purification and Antigenicity of Flavone Synthase I from Irradiated Parsley Cells

2001 ◽  
Vol 393 (1) ◽  
pp. 177-183 ◽  
Author(s):  
Richard Lukačin ◽  
Ulrich Matern ◽  
Kay Teja Junghanns ◽  
Marie-Luise Heskamp ◽  
Lothar Britsch ◽  
...  
Keyword(s):  
Flavone Synthase

scholarly journals Investigation of Two Distinct Flavone Synthases for Plant-Specific Flavone Biosynthesis in Saccharomyces cerevisiae

2005 ◽  
Vol 71 (12) ◽  
pp. 8241-8248 ◽  
Author(s):  
Effendi Leonard ◽  
Yajun Yan ◽  
Kok Hong Lim ◽  
Mattheos A. G. Koffas
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Recombinant Strain ◽  
Plant Secondary Metabolites ◽  
Dependent Manner ◽  
Recombinant Yeast Strain ◽  
Membrane Bound ◽  
Flavone Synthase ◽  
Flavone Synthase Ii ◽  
Dose Dependent

ABSTRACT Flavones are plant secondary metabolites that have wide pharmaceutical and nutraceutical applications. We previously constructed a recombinant flavanone pathway by expressing in Saccharomyces cerevisiae a four-step recombinant pathway that consists of cinnamate-4 hydroxylase, 4-coumaroyl:coenzyme A ligase, chalcone synthase, and chalcone isomerase. In the present work, the biosynthesis of flavones by two distinct flavone synthases was evaluated by introducing a soluble flavone synthase I (FSI) and a membrane-bound flavone synthase II (FSII) into the flavanone-producing recombinant yeast strain. The resulting recombinant strains were able to convert various phenylpropanoid acid precursors into the flavone molecules chrysin, apigenin, and luteolin, and the intermediate flavanones pinocembrin, naringenin, and eriodictyol accumulated in the medium. Improvement of flavone biosynthesis was achieved by overexpressing the yeast P450 reductase CPR1 in the FSII-expressing recombinant strain and by using acetate rather than glucose or raffinose as the carbon source. Overall, the FSI-expressing recombinant strain produced 50% more apigenin and six times less naringenin than the FSII-expressing recombinant strain when p-coumaric acid was used as a precursor phenylpropanoid acid. Further experiments indicated that unlike luteolin, the 5,7,4′-trihydroxyflavone apigenin inhibits flavanone biosynthesis in vivo in a nonlinear, dose-dependent manner.

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