Structural basis for substrate recognition in the <i>Phytolacca americana</i> glycosyltransferase <i>Pa</i>GT3
この論文をさがす
説明
<jats:p>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. <jats:italic>Pa</jats:italic>GT3, a uridine diphosphate glycosyltransferase (UGT) from <jats:italic>Phytolacca americana</jats:italic>, 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 <jats:italic>Pa</jats:italic>GT3 with a sugar-donor analogue (UDP-2-fluoroglucose) and the acceptors capsaicin and kaempferol were determined. <jats:italic>Pa</jats:italic>GT3 adopts a GT-B-fold structure that is highly conserved among UGTs. However, the acceptor-binding pocket in <jats:italic>Pa</jats:italic>GT3 is hydrophobic and large, and is surrounded by longer loops. The larger acceptor-binding pocket in <jats:italic>Pa</jats:italic>GT3 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.</jats:p>
収録刊行物
-
- Acta Crystallographica Section D Structural Biology
-
Acta Crystallographica Section D Structural Biology 78 (3), 379-389, 2022-02-21
International Union of Crystallography (IUCr)