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'Phenylpropanoid Metabolism' in keywords Facet   section ZfN Section C  [X]
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2000 (1)
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1980 (2)
1Author    Dieter StrackRequires cookie*
 Title    Enzymatic Synthesis of 1-Sinapoylglucose from Free Sinapic Acid and UDP-Glucose by a Cell-Free System from Raphanus sativus Seedlings  
 Abstract    Protein extracts from seedlings of Raphanus sativus catalyze the transfer of the glucosyl moiety of UDP-glucose to the carboxyl group o f phenolic acids. Enzymatic activity was determined spec-trophotometrically by measuring the increase in absorbance at 360 nm and/or by the aid of high performance liquid chromatography (HPLC). From 12 phenolic acids tested as acceptors, sinapic acid was by far the best substrate. The glu-cosyltransfer to sinapic acid has a pH optimum near 7 and requires as SH group for activity, p-Chloromercuribenzoate (PCMB) inhibits activity, which can be restored by the addition of di-thiothreitol (DTT). The formation o f 1-sinapoylglucose was found to be a reversible reaction, sin­ ce the addition of UDP results in a breakdown o f the ester. 
  Reference    Z. Naturforsch. 35c, 204—2 (1980); received December 28 1979 
  Published    1980 
  Keywords    Raphanus, Brassicaceae, Phenylpropanoid Metabolism, Glucose Ester, Esterification 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0204.pdf 
 Identifier    ZNC-1980-35c-0204 
 Volume    35 
2Author    Norbert Tkotz, D. Ieter StrackRequires cookie*
 Title    from Raphanus sativus C otyledons  
 Abstract    Protein preparations from cotyledons of Raphanus sati­ vus transfer the sinapoyl moiety of 1 -sinapoylglucose to L-malate to form sinapoyl-L-malate. To our knowledge this is the first time that this type of reaction has been found to be involved in phenylpropanoid depside formation. Most acylation reactions have so far been demonstrated to depend on acyl-CoAs and only one example is known describing 1-O-acyl sugar derivatives as acyl donors. 
  Reference    Z. Naturforsch. 35c, 835—837 (1980); received June 261980 
  Published    1980 
  Keywords    Raphanus, Brassicaceae, Phenylpropanoid Metabolism, Transacylation, Sinapoyltransferase 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0835_n.pdf 
 Identifier    ZNC-1980-35c-0835_n 
 Volume    35 
3Author    Karin Groten, Wolfgang BarzRequires cookie*
 Title    Elicitor-Induced Defence Reactions in Cell Suspension Cultures of Soybean Cultivars  
 Abstract    Suspension cultured soybean (Glycine max [L.] Merr.) cells of four cultivars (Wilis, Lumut, Kalmit, Doko RC) were compared for their response to different fungal and bacterial elici­ tors. Cells were treated either with crude cell wall extracts of the fungal pathogens Phytophth­ ora sojae (Pmg-elicitor) and Rhizoctonia solani (Riso-elicitor) or with two isolates of the bacterial pathogen Pseudomonas syringae pv. glycinea (Psg01/02) and a broad spectrum of antimicrobial defence reactions was measured. Cells of all four cultivars showed the same elicitor-induced rapid (H20 2 accumulation, alkalinization of the culture medium, peroxida-tive cross-linking of cell wall proteins) and slow (activation of phenylpropanoid metabolism, accumulation of phenolic compounds, induction of PR-proteins) defence responses. How­ ever, the reactivity of the cultivars was not identical in terms of time courses and intensities. Furthermore, the ability of the various elicitors to induce defence responses varied markedly. These differences indicate that (1) cells of the same species but of different cultivars are equipped with the same array of perception systems to recognise various stimuli but (2) the sensitivity of these perception systems or later steps in the signal transduction seem to be stimulated to a different extent in the analysed cultivars. 
  Reference    Z. Naturforsch. 55c, 718—730 (2000); received April 25/June 15 2000 
  Published    2000 
  Keywords    Oxidative Burst, PR-Proteins, Phenylpropanoid Metabolism 
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 TEI-XML for    default:Reihe_C/55/ZNC-2000-55c-0718.pdf 
 Identifier    ZNC-2000-55c-0718 
 Volume    55 
4Author    StefanL. Atza, RalfG B ErgerRequires cookie*
 Title    l-0-fra#is-Cinnamoyl-/?-D-glucopyranose: Alcohol Cinnamoyltransferase Activity in Fruits of Cape Gooseberry (Physalis peruviana L.)  
 Abstract    Methyl and ethyl cinnamate are aroma volatiles frequently occurring in fruits. Evidence was obtained that the enzymatic transfer of cinnamic acid to endogenous alcohols present in fruits (methanol, ethanol, 1-propanol) depended on energy-rich 1-O-glycosyl esters of cin­ namic acid which served as acyl donor molecules. A putative 1-O-fra/w-cinnamoyl-^-D-gluco-pyranose; alcohol cinnamoyltransferase from cape gooseberry (Physalis peruviana L.) was active towards l-0-rra«s-cinnamoyl-/3-D-glucopyranose and l-0-rrans-cinnamoyl-/3-D-gentio-biose. The enzyme was purified 290-fold by a protocol including ammonium sulphate precipi­ tation, solubilization by Triton X-100, gel permeation and affinity chromatography on conca-navalin A. The acidic glycoprotein {p i = 4.8) most probably is membrane bound. The distribution of alcohol cinnamoyltransferase activity in gel chromatography fractions suggests a native Mr of 75,000. For l-O-mms-cinnamoyl-ß-D-glucopyranose, an apparent K m of 69 ^im was determined. At pH > 6.0, non-enzymatic transesterification superposes the enzymatic transformation. 
  Reference    Z. Naturforsch. 52c, 747—755 (1997); received June 12/July 28 1997 
  Published    1997 
  Keywords    Phenylpropanoid Metabolism, Glycoconjugate, Flavour Precursor, Aroma Ester, Methyl Cinnamate 
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 TEI-XML for    default:Reihe_C/52/ZNC-1997-52c-0747.pdf 
 Identifier    ZNC-1997-52c-0747 
 Volume    52