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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.

Original publication




Journal article


Nature communications

Publication Date





Key Laboratory of Bio-Resource and Eco-Environment of Ministry of Education, College of Life Sciences, Sichuan University; State Key Laboratory of Biotherapy and Cancer Center, West China Hospital, Sichuan University, 610064, Chengdu, China.


Stevia, Diterpenes, Kaurane, Glycosyltransferases, Glycosides, Glucosides, Glucose, Plant Proteins, Arabidopsis Proteins, Sweetening Agents, Crystallography, X-Ray, Catalytic Domain, Protein Conformation, Substrate Specificity, Catalysis, Hydrophobic and Hydrophilic Interactions