Purification and characterization of (2S)-flavanone 3-hydroxylase from Petunia hybrida
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چکیده
منابع مشابه
Purification and partial characterization of NADPH-cytochrome c reductase from Petunia hybrida flowers.
NADPH-cytochrome c reductase was solubilized from the microsomal fraction of Petunia hybrida flowers by 3-[(3-cholamidopropyl)dimethylammonio]-1-propane sulfonate detergent and purified by adenosine 2',5'-bisphosphate-Sepharose chromatography, followed by high-performance anion-exchange chromatography. Two proteins with molecular sizes of 75 and 81 kD were detected in the purified preparation b...
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Flavanone 3-hydroxylase (F3H) activity is necessary for the biosynthesis of flavonoids, the main ingredients of Gingko biloba extract. The full-length cDNA and genomic DNA sequences of F3H gene were isolated from G. biloba for the first time. The full-length cDNA of G. biloba F3H gene (designated as GbF3H) contained a 1071 bp open reading frame (ORF) encoding a 357-amino-acid protein with a cal...
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A key step in the biosynthesis of flavonoids is the hydroxylation of (2s)-flavanones in the 3 position to form the respective dihydroflavonols. The reaction is catalyzed by F30H, a soluble fraction enzyme requiring 2-oxoglutarate, oxygen, Fez+, and ascorbate for full activity (Heller and Forkmann, 1988). By using genetic mutants that lack F 3 0 H activity, cDNA clones have been identified that ...
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Prolyl 3-hydroxylase was purified up to about 5000-fold from an (NH4)2SO4 fraction of chick-embryo extract by a procedure consisting of affinity chromatography on denatured collagen linked to agarose, elution with ethylene glycol and gel filtration. The molecular weight of the purified enzyme is about 160000 by gel filtration The enzyme is probably a glycoprotein, since (a) its activity is inhi...
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Anthocyanin Biosynthesis, Antirrhinum majus, Flavonoids, Flavanone 3-Hydroxylase, Flavonoid 3'-Hydroxylase, Genetic Control In flower extracts of defined genotypes of Antirrhinum majus, two different hydroxylases were found catalysing the hydroxylation of naringenin and eriodictyol in the 3-position and of naringenin in the 3'-position. The 3-hydroxylase is a soluble enzyme and belongs accordin...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1986
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1986.tb09616.x