Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations

UGT76G1 is an UDP-glucose dependent glycosyltransferase and a component of the biosynthesis pathway for the natural sugar substitute steviol glycoside. Here, the authors present substrate bound crystal structures of UGT76G1 and provide insights into substrate recognition and catalysis by the enzyme.

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Autores principales:	Ting Yang, Jinzhu Zhang, Dan Ke, Wenxian Yang, Minghai Tang, Jian Jiang, Guo Cheng, Jianshu Li, Wei Cheng, Yuquan Wei, Qintong Li, James H. Naismith, Xiaofeng Zhu
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b130fe2e39b3482faa02cb86ccc48a8c
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spelling	oai:doaj.org-article:b130fe2e39b3482faa02cb86ccc48a8c2021-12-02T14:39:35ZHydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations10.1038/s41467-019-11154-42041-1723https://doaj.org/article/b130fe2e39b3482faa02cb86ccc48a8c2019-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11154-4https://doaj.org/toc/2041-1723UGT76G1 is an UDP-glucose dependent glycosyltransferase and a component of the biosynthesis pathway for the natural sugar substitute steviol glycoside. Here, the authors present substrate bound crystal structures of UGT76G1 and provide insights into substrate recognition and catalysis by the enzyme.Ting YangJinzhu ZhangDan KeWenxian YangMinghai TangJian JiangGuo ChengJianshu LiWei ChengYuquan WeiQintong LiJames H. NaismithXiaofeng ZhuNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-12 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Ting Yang Jinzhu Zhang Dan Ke Wenxian Yang Minghai Tang Jian Jiang Guo Cheng Jianshu Li Wei Cheng Yuquan Wei Qintong Li James H. Naismith Xiaofeng Zhu Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations
description	UGT76G1 is an UDP-glucose dependent glycosyltransferase and a component of the biosynthesis pathway for the natural sugar substitute steviol glycoside. Here, the authors present substrate bound crystal structures of UGT76G1 and provide insights into substrate recognition and catalysis by the enzyme.
format	article
author	Ting Yang Jinzhu Zhang Dan Ke Wenxian Yang Minghai Tang Jian Jiang Guo Cheng Jianshu Li Wei Cheng Yuquan Wei Qintong Li James H. Naismith Xiaofeng Zhu
author_facet	Ting Yang Jinzhu Zhang Dan Ke Wenxian Yang Minghai Tang Jian Jiang Guo Cheng Jianshu Li Wei Cheng Yuquan Wei Qintong Li James H. Naismith Xiaofeng Zhu
author_sort	Ting Yang
title	Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations
title_short	Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations
title_full	Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations
title_fullStr	Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations
title_full_unstemmed	Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations
title_sort	hydrophobic recognition allows the glycosyltransferase ugt76g1 to catalyze its substrate in two orientations
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/b130fe2e39b3482faa02cb86ccc48a8c
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Hydrophobic recognition allows the glycosyltransferase UGT76G1 to catalyze its substrate in two orientations

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