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'Chalcone Synthase' in keywords
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1987 (1)
1981 (2)
1Author    Rainer Sütfeld, Rolf WiermannRequires cookie*
 Title    Purification of Chalcone Synthase from Tulip Anthers and Comparison with the Synthase from Cosmos Petals  
 Abstract    Chalcone synthase was isolated from both anthers of Tulipa cv. "A peldoorn" and petals of Cosmos sulphureus Cav. After certain prepurification steps, the enzymes were further purified using gel chrom atography on Sephadex G-200 followed by repeated hydroxylapatite absorption chromatography. Both the enzymes showed the same chrom atographic properties. After gel chrom atography as well as after the first hydroxylapatite fractionation, the reaction products appeared as flavanones. However, after the second hydroxylapatite step, production of chalcones was observed. Like the enzyme from tulip anthers, the synthase from Cosmos petals produced the correspondingly substituted chalcones when p-coumaroyl-CoA, caffeoyl-CoA and feruloyl-CoA, respectively, were used as substractes. In both the cases, the ratios o f the different chalcones produced were found to be about the same. The appearance o f chalcone synthesis in this in vitro assay is caused by the complete elim ination of chalcone isomerase in the purification procedure. The importance of the isomerase for flavonoid biosynthesis, particularly in plant systems which are accumulating chalcones, is discussed. 
  Reference    Z. Naturforsch. 36c, 30—3 (1981); received N ovem ber 12 1980 
  Published    1981 
  Keywords    Tulipa, Cosmos, Biosynthesis, Flavonoids, Chalcone Synthase 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0030.pdf 
 Identifier    ZNC-1981-36c-0030 
 Volume    36 
2Author    R. R. Br, G. Spribille, ForkmRequires cookie*
 Title    Genetic Control of Chalcone Synthase Activity in Flowers of Matthiola incana  
 Abstract    Chalcone synthase activity was demonstrated in enzyme preparations from flowers o f defined genotypes of Matthiola incana (stock). The product formed from 4-coumaroyl-CoA and malonyl-CoA was naringenin and not the isomeric chalcone, because chalcone isomerase was also present in the reaction mixture. Chalcone synthase activity could be detected only in flower extracts o f genotypes with wild-type alleles at the locus f Thus, the interruption of the anthocyanin pathway in white flowering lines with recessive alleles (ff) of this gene is clearly due to a lack o f this enzyme activity. Independent on the genetic state of the locus b which controls the formation of pelargonidin or cyanidin, respectively, in the flowers, 4-coumaroyl-CoA was the only suitable substrate for the condensation reaction. 
  Reference    Z. Naturforsch. 36c, 619 (1981); received April 3 1981 
  Published    1981 
  Keywords    Anthocyanins, Flavonoids, Chalcone Synthase, Genetic Control, Matthiola incana 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0619.pdf 
 Identifier    ZNC-1981-36c-0619 
 Volume    36 
3Author    K. Stich, G. ForkmRequires cookie*
 Title    Enzymatic Synthesis of 4'-and 3 ' ,4 -Hydroxylated Flavanones and Flavones with Flower Extracts of Sinningia cardinalis  
 Abstract    Flowers o f Sinningia (syn. Rechsteineria) cardinalis contain glycosides of the flavones apigenin (4'-O H) and luteolin (3',4'-O H) respectively, and of the related 3-deoxyanthocyanidins apigenin-idin and luteolinidin. Studies on substrate specificity of the key enzym e o f flavonoid biosynthesis, chalcone synthase, revealed that the 3',4'-hydroxylated flavonoids are formed by hydroxylation o f flavonoid com pounds rather than by incorporation of caffeoyl-C oA into the flavonoid skeleton during the condensation reaction. In fact, flavonoid 3'-hydroxylase activity could be dem onstrat­ ed in the m icrosom al fraction o f the flower extracts. The enzym e catalyses hydroxylation of naringenin and apigenin in the 3'-position to eriodictyol and luteolin, respectively, with N A D P H as cofactor. B esides flavanone 3'-hydroxylase a further N A D P H -d ep en dent enzym e activity (fla­ vone synthase II) was observed in the microsomal fraction catalysing the oxidation o f naringenin to apigenin and o f eriodictyol to luteolin. The Cytochrome P-450 inhibitor ancymidol was found to abolish com pletely flavone synthase II activity, whereas flavonoid 3'-hydroxylase activity was not impaired. 
  Reference    Z. Naturforsch. 42c, 1193 (1987); received July 9/August 19 1987 
  Published    1987 
  Keywords    Flavonoid B iosynthesis, Chalcone Synthase, Flavonoid 3'-H ydroxylase, Flavone Synthase II, Sinningia cardinalis 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-1193.pdf 
 Identifier    ZNC-1987-42c-1193 
 Volume    42