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. 2024 Jun 28;7:147. doi: 10.1038/s42004-024-01231-1

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a Reaction scheme from sinapic acid to the corresponding 4-O-glucoside catalyzed by UGT72 enzymes (UGT72D1, UGT72D7), or to glucose-1-ester catalyzed by UGT84 members (UGT84A119, UGT84A49). b Overlay of HPLC chromatograms (24 h time point) from UGT84A119/UGT84A49 reactions with sinapic acid at pH 5.0 and 8.0. c Overlaid HPLC chromatograms (24 h time point) from UGT72D1/UGT72D7 reactions with sinapic acid at pH 5.0 and 8.0. d Time courses of product formation in UGT/sinapic acid reactions used for measuring the enzymatic activities. Reactions (100 μL) contained 1.0 mM sinapic acid, 2.0 mM UDP-Glc and 0.0050-0.50 mg mL⁻¹ enzyme in 50 mM potassium phosphate buffer (pH 5.0 or 8.0).