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

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 () and Xiaofeng Zhu ()
Additional contact information
Ting Yang: Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University
Jinzhu Zhang: Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University
Dan Ke: Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University
Wenxian Yang: Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University
Minghai Tang: West China Hospital, Sichuan University
Jian Jiang: Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University
Guo Cheng: West China School of Public Health, Healthy Food Evaluation Research Center and State Key Laboratory of Biotherapy and Cancer Center, Sichuan University
Jianshu Li: College of Polymer Science and Engineering and State Key Laboratory of Polymer Materials Engineering, Sichuan University
Wei Cheng: West China Hospital, Sichuan University
Yuquan Wei: West China Hospital, Sichuan University
Qintong Li: Ministry of Education, Sichuan University
James H. Naismith: West China Hospital, Sichuan University
Xiaofeng Zhu: Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University

Nature Communications, 2019, vol. 10, issue 1, 1-12

Abstract: Abstract Diets high in sugar are recognized as a serious health problem, and there is a drive to reduce their consumption. Steviol glycosides are natural zero-calorie sweeteners, but the most desirable ones are biosynthesized with low yields. UGT76G1 catalyzes the β (1–3) addition of glucose to steviol glycosides, which gives them the preferred taste. UGT76G1 is able to transfer glucose to multiple steviol substrates yet remains highly specific in the glycosidic linkage it creates. Here, we report multiple complex structures of the enzyme combined with biochemical data, which reveal that the enzyme utilizes hydrophobic interactions for substrate recognition. The lack of a strict three-dimensional recognition arrangement, typical of hydrogen bonds, permits two different orientations for β (1–3) sugar addition. The use of hydrophobic recognition is unusual in a regio- and stereo-specific catalysis. Harnessing such non-specific hydrophobic interactions could have wide applications in the synthesis of complex glycoconjugates.

Date: 2019
References: Add references at CitEc
Citations: View citations in EconPapers (4)

Downloads: (external link)
https://www.nature.com/articles/s41467-019-11154-4 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-11154-4

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-019-11154-4

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().