ArticlePlanta2026
Identification and functional characterization of UDP-glycosyltransferases catalyzing the glycosylation of oleoside 11-methyl ester in Olea europaea.
Article in Planta, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
MAIN
conclusionTwo UDP-glycosyltransferases from Olea europaea were identified and characterized. Both catalyze the glycosylation of oleoside 11-methyl ester to form 7-β-1-D-glucopyranosyl 11-methyl oleoside, a putative intermediate in the oleuropein biosynthetic pathway.
introductionOleuropein, a secoiridoid glycoside abundant in Oleaceae plants, is extensively utilized in the pharmaceutical, nutraceutical, and cosmetic industries due to its diverse pharmacological activities. The biosynthetic pathway from oleoside 11-methyl ester (OME) to oleuropein remains incompletely elucidated. In this study, two UDP-glycosyltransferases (UGTs), OeUGT1and OeUGT2, were identified in O. europaea. First, based on differential expression analysis and the characteristics of enzymes catalyzing carboxyl glycosylation, 51 differentially expressed UGTs were narrowed to 6 candidates. Both in vivo and in vitro enzyme activity assays demonstrated that OeUGT1 could catalyze OME to 7-β-1-D-glucopyranosyl 11-methyl oleoside (OME-Glc). The enzymatic properties of OeUGT1 were then characterized. The optimal reaction temperature was found to be 30 °C, and the optimal pH was 6.0. OeUGT1 exhibited a Michaelis constant (K
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