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Review Article

The Advances and Challenges in Enzymatic <i>C</i>-glycosylation of Flavonoids in Plants

[ Vol. 28 , Issue. 18 ]


Hui-Yao Gao, Yan Liu, Fei-Fan Tan, Li-Wen Zhu, Kai-Zhi Jia* and Ya-Jie Tang   Pages 1466 - 1479 ( 14 )


Flavonoid glycosides play determinant roles in plants and have considerable potential for applications in medicine and biotechnology. Glycosyltransferases transfer a sugar moiety from uridine diphosphateactivated sugar molecules to an acceptor flavonoid via C-O and C-C linkages. Compared with O-glycosyl flavonoids, C-glycosyl flavonoids are more stable, resistant to glycosidase or acid hydrolysis, exhibit better pharmacological properties, and have received more attention. In this study, we discuss the mining of C-glycosyl flavones and the corresponding C-glycosyltransferases and evaluate the differences in structure and catalytic mechanisms between C-glycosyltransferase and O-glycosyltransferase. We conclude that promiscuity and specificity are key determinants for general flavonoid C-glycosyltransferase engineering and summarize the C-glycosyltransferase engineering strategy. A thorough understanding of the properties, catalytic mechanisms, and engineering of C-glycosyltransferases will be critical for future biotechnological applications in areas such as the production of desired C-glycosyl flavonoids for nutritional or medicinal use.


Flavonoid glycosyltransferase, O-glycosyltransferase, catalytic mechanism, promiscuity, specificity engineering, c-glycosylation.


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