Language selection

Government of Canada / Gouvernement du Canada

Search

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

From National Research Council Canada

DOIResolve DOI: https://doi.org/10.1016/S0031-9422(00)89867-2
AuthorSearch for: 1; Search for: 1
Affiliation
  1. National Research Council of Canada. Prairie Regional Laboratory
FormatText, Article
Abstract
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.
Publication date
PublisherElsevier
Pergamon Press
In
  • Phytochemistry 10, no. 10 (October 1971): 2279–2286.
LanguageEnglish
Peer reviewedYes
IdentifierS0031942200898672
NRCC-12067
Export citationExport as RIS
Report a correctionReport a correction (opens in a new tab)
Record identifier002b951d-e1ab-4c2e-a091-4faec5c385f2
Record created2023-10-17
Record modified2023-10-17
Date modified: