Purification and Properties of UDP-Glucose: Thiohydroximate Glucosyltransferase from Brassica napus L. Seedlings

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DOIResolve DOI: http://doi.org/10.1006/abbi.1993.1456
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TypeArticle
Journal titleArchives of Biochemistry
ISSN0096-9621
Volume305
Issue2
Pages526532; # of pages: 7
SubjectUDP-Glucose; Brassica napus; purification
AbstractA uridinediphosphateglucose:thiohydroximate glucosyltransferase (EC 2.4.1.-) has been purified 3700-fold from Brassica napus L. seedlings. The enzyme catalyzes the formation of desulfoglucosinolates by transfer of glucose from UDP-glucose to thiohydroximates and is believed to be the second to last step involved in glucosinolate biosynthesis. The enzyme was purified to near homogeneity, exhibiting a single band by non-denaturing polyacrylamide gel electrophoresis (PAGE) and on sodium dodecyl sulfate-PAGE (Mr 46,000) but showed multiple isoforms between pH 4.6 and 4.3 when resolved by IEF. The enzyme is stable at temperatures up to 30°C for at least 1 h and shows maximum activity rates at pH 6.0 and has no absolute requirements for cations. The Km values for UDP-glucose and phenylacetothiohydroximate were calculated to be 0.46 and 0.05 mM, respectively. This enzyme possesses a high degree of specificity for the thiohydroximic functional group but little specificity for the associated side-chain groups. Similar enzyme activity has been detected in all other members of the Brassicaceae family tested and is believed to be a common thiohydroximate glucosylating enzyme present in these and other glucosinolate producing plants.
Publication date
LanguageEnglish
AffiliationNRC Plant Biotechnology Institute; National Research Council Canada
Peer reviewedYes
NRC number36488
NPARC number21275383
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Record identifier8b52391e-c718-40dc-bf15-e6d2bb2d3fbb
Record created2015-06-24
Record modified2016-05-09
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