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

TY - JOUR

T1 - The use of abscisic acid analogues to analyse the substrate selectivity of UGT71B6, a UDP-glycosyltransferase of Arabidopsis thaliana

AU - Priest, D M

AU - Jackson, R G

AU - Ashford, D A

AU - Abrams, S R

AU - Bowles, D J

PY - 2005/8/15

Y1 - 2005/8/15

N2 - 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.

AB - 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.

KW - glycosyltransferase

KW - abscisic acid

KW - glucose ester

KW - analogues

KW - enantiomer

KW - Arabidopsis thaliana

KW - (+)-ABSCISIC ACID

KW - BIOLOGICAL-ACTIVITY

KW - GLUCOSYLTRANSFERASE

KW - ABA

KW - IDENTIFICATION

KW - 8'-HYDROXYLASE

KW - GERMINATION

KW - METABOLISM

KW - GENE

KW - INHIBITION

U2 - 10.1016/j.febslet.2005.06.084

DO - 10.1016/j.febslet.2005.06.084

M3 - Article

SN - 0014-5793

VL - 579

SP - 4454

EP - 4458

JO - FEBS Letters

JF - FEBS Letters

IS - 20

ER -