What question did this study set out to answer?

This research examines how segmental duplication influences the functional diversification of UDP-glycosyltransferases in Polygonum cuspidatum.

June 15, 2026

Functional Divergence of Three Segmentally Duplicated UGT71 Enzymes Reveals Distinct Glycosylation Strategies toward Resveratrol and Emodin in Polygonum cuspidatum

Puntos clave

This research examines how segmental duplication influences the functional diversification of UDP-glycosyltransferases in Polygonum cuspidatum.
Identified and classified 186 PcUGTs into 17 phylogenetic groups based on segmental duplication.
Characterized functional divergence of PcUGT71AH6 and PcUGT71U25 enzymes toward glycosylation activity.
Performed docking and molecular dynamics simulations to analyze enzyme-substrate interactions.
PcUGT71AH6 showed no significant glycosylation activity toward resveratrol or emodin.
PcUGT71U25 demonstrated promiscuous glycosylation towards emodin with notable deglycosylation activity.
E86A mutation in PcUGT71U25 improved site selectivity for C1-OH by altering substrate binding.

Resumen

Polygonum cuspidatum is a medicinal and edible plant rich in bioactive phenolics, predominantly occurring as O -glycosides catalyzed by UDP-glycosyltransferases (UGTs). However, how gene duplication drives the UGT functional diversification remains unclear. Here, 186 PcUGTs were identified and classified into 17 phylogenetic groups with segmental duplication as the primary driver of family expansion. Two segmentally duplicated paralogs of the previously characterized PcUGT71BE11, namely, PcUGT71AH6 and PcUGT71U25, exhibited pronounced functional divergence. PcUGT71AH6 showed no detectable glycosylation activity toward resveratrol or emodin under the tested conditions. In contrast, PcUGT71U25 displayed site-promiscuous glycosylation toward emodin and UDP-dependent deglycosylation activity toward its glycosides. Docking and molecular dynamics simulations revealed a conformationally adaptable active pocket in PcUGT71U25 that accommodates multiple productive emodin binding poses. Notably, the E86A mutation enhanced C1-OH site selectivity by reshaping substrate binding conformations. Overall, this study provides mechanistic insights into UGT diversification and phenolic glycoside biosynthesis in P. cuspidatum .

Me gusta

Guardar