| 2 | Author
| D. Ieter, Strack An, M. Aria Bokern, Jochen Berlin An D, Sabine Sieg | Requires cookie* | | Title
| Metabolie Activity of Hydroxycinnamic Acid Glucose Esters in Cell Suspension Cultures of Chenopodium rubrum  | | | Abstract
| Cell suspension cultures o f Chenopodium rubrum accumulate high amounts of metabolically active glucose esters of ^?-coumaric and ferulic acid. Pulse-labelling experiments using [14C]phe-nylalanine and application o f the phenylalanine ammonia-lyase (PAL) inhibitor L-a-aminooxy-/3-pnenylpropionic acid (AOPP) revealed that the glucose esters are subject to high turnover. A considerable portion o f the ferulic acid was found as an insoluble component, probably bound to cell wall material. Application of m-fluoro-DL-tyrosine (MFT), an effective inhibitor o f tyrosine biosynthesis via L-arogenate, markedly increased the amount of 1-p-coumaroyl-and 1-feruloyl-glucose accumulated. | | |
Reference
| Z. Naturforsch. 39c, 902—907 (1984); received May 16 1984 | | |
Published
| 1984 | | |
Keywords
| Chenopodium rubrum, Cell Culture, Hydroxycinnamic Acid, Glucose Ester, Betalain | | |
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| | | | TEI-XML for
| default:Reihe_C/39/ZNC-1984-39c-0902.pdf | | | Identifier
| ZNC-1984-39c-0902 | | | Volume
| 39 | |
3 | Author
| A. Fleuriet, J. J. Macheix, R. Suen, R. K. Ibrahim | Requires cookie* | | Title
| Partial Purification and Some Properties of a Hydroxycinnamoyl Glucosyltransferase from Tomato Fruits  | | | Abstract
| A glucosyltransferase was isolated from im mature "cherry" tom atoes and was partially purified (200-fold) by am m onium sulphate precipitation and successive chrom atography on Sephadex G-100 and DEAE-cellulose columns. The enzyme utilised the free hydroxycinnamic acids and UDP-glucose in the form ation o f their respective glucosides (pH 8.0) and glucose esters (pH 7.0); but did not accept the CoA thiolesters o f HCAs in the presence of glucose-1-phosphate. The constant glucoside/glucose ester ratio observed during purification suggests that both reactions are catalysed by the sam e enzyme. The K m values for /»-coumaric, caffeic, ferulic and sinapic acids were 0.8, 1.5, 1.4 and 2.5 hm, respectively. W ith ferulic acid as substrate, the K m value for U D PG was 10 hm. The enzyme required an -S H group for activity and the reaction was strongly inhibited by EDTA, divalent metal ions and UDP. | | |
Reference
| Z. Naturforsch. 35c, 967—9 (1980); received August 14 1980 | | |
Published
| 1980 | | |
Keywords
| Glucosyltransferase, Glucosides, Glucose Esters, Hydroxycinnamic Acids, Enzyme Purification and Properties, Tom ato Fruit, Lycopersicum esculentum (Solanaceae) | | |
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| default:Reihe_C/35/ZNC-1980-35c-0967.pdf | | | Identifier
| ZNC-1980-35c-0967 | | | Volume
| 35 | |
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