Functional Characterization of a Novel Glycosyltransferase (UGT73CD1) from Iris tectorum Maxim. for the Substrate promiscuity
Autor: | Jianlian Wu, Libing Zhang, Li Jing, Jincai Liang, Lixin Duan, Jia Huang, Zilu Huang, Wei Yao, Aijia Ji, Jingyang Yue, Rui Guan |
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Rok vydání: | 2021 |
Předmět: |
Tectorigenin
Glycosylation Iris Plant Flavonoid Bioengineering Computational biology Tectoridin Applied Microbiology and Biotechnology Biochemistry Substrate Specificity Transcriptome chemistry.chemical_compound Glycosyltransferase Iris tectorum Amino Acid Sequence Glycosides Molecular Biology Phylogeny Plant Proteins Flavonoids chemistry.chemical_classification Sequence Homology Amino Acid biology Phylogenetic tree Drug discovery fungi Glycosyltransferases food and beverages biology.organism_classification Isoflavones chemistry biology.protein Biotechnology |
Zdroj: | Molecular Biotechnology. 63:1030-1039 |
ISSN: | 1559-0305 1073-6085 |
DOI: | 10.1007/s12033-021-00364-1 |
Popis: | 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. |
Databáze: | OpenAIRE |
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