ArticleActa crystallographica. Section D, Structural biology2022
Structural basis for substrate recognition in the Phytolacca americana glycosyltransferase PaGT3.
Article in Acta crystallographica. Section D, Structural biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Article
- A Near Telomere-To-Telomere Genome Assembly of Coffea arabica (Mundo Novo) Provides Insights Into Its Secondary Metabolism.Molecular ecology resources · 2025Article
- Single-crystal structure of the spicy capsaicin.Acta crystallographica. Section C, Structural chemistry · 2025Article
- Structural Insights into the Substrate Recognition of Ginsenoside Glycosyltransferase Pq3-O-UGT2.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Insights from Structure-Based Simulations into the Persulfidation of Uridine Diphosphate-Glycosyltransferase71c5 Facilitating the Reversible Inactivation of Abscisic Acid.International journal of molecular sciences · 2024Article
- Supramolecular Synthons in Protein-Ligand Frameworks.Crystal growth & design · 2024Article
- Similarities in Structure and Function of UDP-Glycosyltransferase Homologs from Human and Plants.International journal of molecular sciences · 2024Review
- Structure-function and engineering of plant UDP-glycosyltransferase.Computational and structural biotechnology journal · 2023Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Capsaicinoids are phenolic compounds that have health benefits. However, the pungency and poor water solubility of these compounds limit their exploitation. Glycosylation is a powerful method to improve water solubility and reduce pungency while preserving bioactivity. PaGT3, a uridine diphosphate glycosyltransferase (UGT) from Phytolacca americana, is known for its ability to glycosylate capsaicinoids and other phenolic compounds. While structural information on several UGTs is available, structures of UGTs that can glycosylate a range of phenolic compounds are rare. To fill this gap, crystal structures of PaGT3 with a sugar-donor analogue (UDP-2-fluoroglucose) and the acceptors capsaicin and kaempferol were determined. PaGT3 adopts a GT-B-fold structure that is highly conserved among UGTs. However, the acceptor-binding pocket in PaGT3 is hydrophobic and large, and is surrounded by longer loops. The larger acceptor-binding pocket in PaGT3 allows the enzyme to bind a range of compounds, while the flexibility of the longer loops possibly plays a role in accommodating the acceptors in the binding pocket according to their shape and size. This structural information provides insights into the acceptor-binding mechanism in UGTs that bind multiple substrates.
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