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Structural basis for substrate recognition in the Phytolacca americana glycosyltransferase PaGT3
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 g...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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International Union of Crystallography
2022
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8900826/ https://www.ncbi.nlm.nih.gov/pubmed/35234151 http://dx.doi.org/10.1107/S2059798322000869 |
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author | Maharjan, Rakesh Fukuda, Yohta Nakayama, Taisuke Nakayama, Toru Hamada, Hiroki Ozaki, Shin-ichi Inoue, Tsuyoshi |
author_facet | Maharjan, Rakesh Fukuda, Yohta Nakayama, Taisuke Nakayama, Toru Hamada, Hiroki Ozaki, Shin-ichi Inoue, Tsuyoshi |
author_sort | Maharjan, Rakesh |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-8900826 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | International Union of Crystallography |
record_format | MEDLINE/PubMed |
spelling | pubmed-89008262022-03-29 Structural basis for substrate recognition in the Phytolacca americana glycosyltransferase PaGT3 Maharjan, Rakesh Fukuda, Yohta Nakayama, Taisuke Nakayama, Toru Hamada, Hiroki Ozaki, Shin-ichi Inoue, Tsuyoshi Acta Crystallogr D Struct Biol Research Papers 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. International Union of Crystallography 2022-02-21 /pmc/articles/PMC8900826/ /pubmed/35234151 http://dx.doi.org/10.1107/S2059798322000869 Text en © Rakesh Maharjan et al. 2022 https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
spellingShingle | Research Papers Maharjan, Rakesh Fukuda, Yohta Nakayama, Taisuke Nakayama, Toru Hamada, Hiroki Ozaki, Shin-ichi Inoue, Tsuyoshi Structural basis for substrate recognition in the Phytolacca americana glycosyltransferase PaGT3 |
title | Structural basis for substrate recognition in the Phytolacca americana glycosyltransferase PaGT3 |
title_full | Structural basis for substrate recognition in the Phytolacca americana glycosyltransferase PaGT3 |
title_fullStr | Structural basis for substrate recognition in the Phytolacca americana glycosyltransferase PaGT3 |
title_full_unstemmed | Structural basis for substrate recognition in the Phytolacca americana glycosyltransferase PaGT3 |
title_short | Structural basis for substrate recognition in the Phytolacca americana glycosyltransferase PaGT3 |
title_sort | structural basis for substrate recognition in the phytolacca americana glycosyltransferase pagt3 |
topic | Research Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8900826/ https://www.ncbi.nlm.nih.gov/pubmed/35234151 http://dx.doi.org/10.1107/S2059798322000869 |
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