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'Glucosyltransferase' in keywords
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1980 (1)
1979 (1)
1Author    JosieL. Shute, PabloS. Jourdan, RichardL. MansellRequires cookie*
 Title    UDP-Glucose: Glucosyltransferase Activity Involved in the Biosynthesis of Flavonol Triglucosides in Pisum sativum L. Seedlings  
 Abstract    From young, light-grown seedlings o f Pisum sativum L. an enzyme activity catalyzing the glu-cosylation o f kaempferol and quercetin in the 3-position to form the 3-0-triglucoside derivative has been demonstrated. The reaction proceeds from the aglycone via the mono-and diglucoside intermediates. The triglucoside can be produced from any o f the less substituted derivatives with uridine diphosphate-Z)-glucose (U D P G) as the glucosyl donor. Young leaf tissues had much high­ er levels o f glucosyltransferase activity than the petioles and internodes. This is the first report o f the synthesis o f flavonol-3-0-triglucosides in vitro. 
  Reference    Z. Naturforsch. 34c, 738 (1979); received June 25 1979 
  Published    1979 
  Keywords    Pisum sativum, Peas, Flavonols, Triglucosides, Glucosyltransferase 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0738.pdf 
 Identifier    ZNC-1979-34c-0738 
 Volume    34 
2Author    A. Fleuriet, J. J. Macheix, R. Suen, R. K. IbrahimRequires 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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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0967.pdf 
 Identifier    ZNC-1980-35c-0967 
 Volume    35