4.4 Article

Functional Characterization of a Novel Glycosyltransferase (UGT73CD1) from Iris tectorum Maxim. for the Substrate promiscuity

Journal

MOLECULAR BIOTECHNOLOGY
Volume 63, Issue 11, Pages 1030-1039

Publisher

SPRINGERNATURE
DOI: 10.1007/s12033-021-00364-1

Keywords

Iris tectorum Maxim; Tectoridin; Isoflavones; Glycosyltransferase; Heterologous expression

Funding

  1. Guangdong Key Laboratory for translational Cancer research of Chinese Medicine [2018B030322011]
  2. National Natural Science Foundation of China (CN) [81874333, 82003895]
  3. Guangdong Basic and Applied Basic Research Foundation [2020A1515010926]

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UGT73CD1, identified from Iris tectorum, is a novel glycosyltransferase with broad catalytic promiscuity towards various substrates. This study provides insights into efficient biosynthesis of structurally diverse flavonoid glycosides for drug discovery.
Glycosylflavonoids are a class of natural products with multiple pharmacological activities and a lot of glycosyltransferases from various plant species have been reported that they were involved in the biosynthesis of these phytochemicals. However, no corresponding glycosyltransferase has been identified from the famous horticultural and medicinal plant Iris tectorum Maxim. Here, UGT73CD1, a novel glycosyltransferase, was identified from I. tectorum. based on transcriptome analysis and functional identification. Phylogenetic analysis revealed that UGT73CD1 grouped into the clade of flavonoid 7-OH OGTs. Biochemical analysis showed that UGT73CD1 was able to glycosylate tectorigenin at 7-OH to produce tectoridin, and thus assigned as a 7-O-glycosyltransferase. In addition, it also possessed robust catalytic promiscuity toward 12 structurally diverse flavonoid scaffolds and 3, 4-dichloroaniline, resulting in forming O- and N-glycosides. This work will provide insights into efficient biosynthesis of structurally diverse flavonoid glycosides for drug discovery.

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