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Purification and properties of a UDP glucose: Thiohydroximate glucosyltransferase from higher plants

DOITrouver le DOI : https://doi.org/10.1016/S0031-9422(00)89867-2
AuteurRechercher : 1; Rechercher : 1
Affiliation
  1. Conseil national de recherches du Canada. Laboratoire régional des prairies
FormatTexte, Article
Résumé
An enzyme which catalyses the formation of desulfobenzylglucosinolate by glucosyl transfer from UDP glucose to phenylacetothiohydroximate has been isolated from leaves of Tropaeolum majus L. and purified 20-fold. The enzyme possessed a high degree of specificity for the sugar acceptor molecule (thiohydroximates), the donor nucleotide (UPD) and its sugar (glucose). The activity of the enzyme was increased by sulfhydryl, chelating and reducing compounds: the activity disappeared in the absence of β-mercaptoethanol and was strongly inhibited by mercuric chloride and p-chloromercuribenzoate. Cell-free extracts of other glucosinolate-containing plants, including Sinapis alba L., Nasturtium officinale R. Br. and Armoracia lapathifolia Gilib. contained a similar glucosyl-transferase activity. It is concluded that the glycosylation of phenylacetothiohydroximate is an integral step in the biosynthesis of benzylglucosinolate.
Date de publication
Maison d’éditionElsevier
Pergamon Press
Dans
  • Phytochemistry 10, nº 10 (octobre 1971) : 2279–2286.
Langueanglais
Publications évaluées par des pairsOui
IdentificateurS0031942200898672
NRCC-12067
Exporter la noticeExporter en format RIS
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Identificateur de l’enregistrement002b951d-e1ab-4c2e-a091-4faec5c385f2
Enregistrement créé2023-10-17
Enregistrement modifié2023-10-17

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