Abstract
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 .
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Claims 7
Claim · model-written summary
The study identified 186 PcUGTs in 17 phylogenetic groups.
- Taxon
- Polygonum cuspidatum
Polygonum cuspidatumt0 - Gene
- PcUGTse0
- Outcome
- identified and classified into 17 phylogenetic groupse0
- Value
- 186e0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“186 PcUGTs were identified and classified into 17 phylogenetic groups”
t0“Polygonum cuspidatum”
Claim · model-written summary
Segmental duplication was the primary driver of PcUGT family expansion.
- Taxon
- Polygonum cuspidatumPolygonum cuspidatumt0
- Outcome
- family expansione0
- Qualifier
- segmental duplicatione0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“segmental duplication as the primary driver of family expansion”
t0“Polygonum cuspidatum”
Claim · model-written summary
PcUGT71AH6 showed no detectable glycosylation of resveratrol or emodin under tested conditions.
- Taxon
- Polygonum cuspidatumPolygonum cuspidatumt0
- Gene
- PcUGT71AH6e0
- Outcome
- no detectable glycosylation activity toward resveratrol or emodine0
- Qualifier
- under the tested conditionse0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“PcUGT71AH6 showed no detectable glycosylation activity toward resveratrol or emodin under the tested conditions”
t0“Polygonum cuspidatum”
Claim · model-written summary
PcUGT71U25 glycosylated emodin at multiple sites.
- Taxon
- Polygonum cuspidatumPolygonum cuspidatumt0
- Gene
- PcUGT71U25e0
- Outcome
- site-promiscuous glycosylation toward emodine0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“PcUGT71U25 displayed site-promiscuous glycosylation toward emodin”
t0“Polygonum cuspidatum”
Claim · model-written summary
PcUGT71U25 had UDP-dependent deglycosylation activity toward emodin glycosides.
- Taxon
- Polygonum cuspidatumPolygonum cuspidatumt0
- Gene
- PcUGT71U25e0
- Outcome
- UDP-dependent deglycosylation activity toward its glycosidese0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“PcUGT71U25 displayed site-promiscuous glycosylation toward emodin and UDP-dependent deglycosylation activity toward its glycosides”
t0“Polygonum cuspidatum”
Claim · model-written summary
Simulations indicated that the adaptable PcUGT71U25 pocket accommodates multiple productive emodin poses.
- Taxon
- Polygonum cuspidatumPolygonum cuspidatumt0
- Gene
- PcUGT71U25e0
- Outcome
- multiple productive emodin binding posese0
- Qualifier
- a conformationally adaptable active pockete0
Not reportedDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Docking and molecular dynamics simulations revealed a conformationally adaptable active pocket in PcUGT71U25 that accommodates multiple productive emodin binding poses”
t0“Polygonum cuspidatum”
Claim · model-written summary
The E86A mutation enhanced C1-OH site selectivity by reshaping substrate binding conformations.
- Taxon
- Polygonum cuspidatumPolygonum cuspidatumt0
- Gene
- E86Ae0
- Outcome
- C1-OH site selectivitye0
- Direction
- enhancede0
- Qualifier
- reshaping substrate binding conformationse0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“the E86A mutation enhanced C1-OH site selectivity by reshaping substrate binding conformations”
t0“Polygonum cuspidatum”