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The use of abscisic acid analogues to analyse the substrate selectivity of UGT71B6, a UDP-glycosyltransferase of Arabidopsis thaliana

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Published copy (DOI)

Author(s)

  • D M Priest
  • R G Jackson
  • D A Ashford
  • S R Abrams
  • D J Bowles

Department/unit(s)

Publication details

JournalFEBS Letters
DatePublished - 15 Aug 2005
Issue number20
Volume579
Number of pages5
Pages (from-to)4454-4458
Original languageEnglish

Abstract

This study analyses the activity of an Arabidopsis thaliana UDP-glycosyltransferase, UGT71B6 (71116), towards abscisic acid (ABA) and its structural analogues. The enzyme preferentially glucosylated ABA and not its catabolites. The requirement for a specific chiral configuration of (+)-ABA was demonstrated through the use of analogues with the chiral centre changed or removed. The enzyme was able to accommodate extra bulk around the double bond of the ABA ring but not alterations to the 8'- and 9'- methyl groups. Interestingly, the ketone of ABA was not required for glucosylation. Bioactive analogues, resistant to 8'-hydroxylation, were also poor substrates for conjugation by UGT71B6. This suggests the compounds may be resistant to both pathways of ABA inactivation and may, therefore, prove to be useful agrochemicals for field applications. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.

    Research areas

  • glycosyltransferase, abscisic acid, glucose ester, analogues, enantiomer, Arabidopsis thaliana, (+)-ABSCISIC ACID, BIOLOGICAL-ACTIVITY, GLUCOSYLTRANSFERASE, ABA, IDENTIFICATION, 8'-HYDROXYLASE, GERMINATION, METABOLISM, GENE, INHIBITION

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