Identification and Characterization of Two Bibenzyl Glycosyltransferases from the Liverwort <i>Marchantia polymorpha</i>
Liverworts are rich in bibenzyls and related <i>O</i>-glycosides, which show antioxidant activity. However, glycosyltransferases that catalyze the glycosylation of bibenzyls have not yet been characterized. Here, we identified two bibenzyl UDP-glucosyltransferases named <i>Mp</i...
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MDPI AG
2022-04-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/11/4/735 |
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| author | Rui-Lin Xiong Jiao-Zhen Zhang Xin-Yan Liu Jian-Qun Deng Ting-Ting Zhu Rong Ni Hui Tan Ju-Zheng Sheng Hong-Xiang Lou Ai-Xia Cheng |
| author_facet | Rui-Lin Xiong Jiao-Zhen Zhang Xin-Yan Liu Jian-Qun Deng Ting-Ting Zhu Rong Ni Hui Tan Ju-Zheng Sheng Hong-Xiang Lou Ai-Xia Cheng |
| author_sort | Rui-Lin Xiong |
| collection | DOAJ |
| description | Liverworts are rich in bibenzyls and related <i>O</i>-glycosides, which show antioxidant activity. However, glycosyltransferases that catalyze the glycosylation of bibenzyls have not yet been characterized. Here, we identified two bibenzyl UDP-glucosyltransferases named <i>Mp</i>UGT737B1 and <i>Mp</i>UGT741A1 from the model liverwort <i>Marchantia polymorpha</i>. The in vitro enzymatic assay revealed that <i>Mp</i>UGT741A1 specifically accepted the bibenzyl lunularin as substrate. <i>Mp</i>UGT737B1 could accept bibenzyls, dihydrochalcone and phenylpropanoids as substrates, and could convert phloretin to phloretin-4-<i>O</i>-glucoside and phloridzin, which showed inhibitory activity against tyrosinase and antioxidant activity. The results of sugar donor selectivity showed that <i>Mp</i>UGT737B1 and <i>Mp</i>UGT741A1 could only accept UDP-glucose as a substrate. The expression levels of these <i>Mp</i>UGTs were considerably increased after UV irradiation, which generally caused oxidative damage. This result indicates that <i>Mp</i>UGT737B1 and <i>Mp</i>UGT741A1 may play a role in plant stress adaption. Subcellular localization indicates that <i>Mp</i>UGT737B1 and <i>Mp</i>UGT741A1 were expressed in the cytoplasm and nucleus. These enzymes should provide candidate genes for the synthesis of bioactive bibenzyl <i>O</i>-glucosides and the improvement of plant antioxidant capacity. |
| first_indexed | 2024-03-09T11:14:16Z |
| format | Article |
| id | doaj.art-b52061df8be34345b02a636b824cd989 |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-09T11:14:16Z |
| publishDate | 2022-04-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-b52061df8be34345b02a636b824cd9892023-12-01T00:36:01ZengMDPI AGAntioxidants2076-39212022-04-0111473510.3390/antiox11040735Identification and Characterization of Two Bibenzyl Glycosyltransferases from the Liverwort <i>Marchantia polymorpha</i>Rui-Lin Xiong0Jiao-Zhen Zhang1Xin-Yan Liu2Jian-Qun Deng3Ting-Ting Zhu4Rong Ni5Hui Tan6Ju-Zheng Sheng7Hong-Xiang Lou8Ai-Xia Cheng9Key Laboratory of Chemical Biology of Natural Products (Ministry of Education), School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, ChinaKey Laboratory of Chemical Biology of Natural Products (Ministry of Education), School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, ChinaDepartment of Pharmacy, Qilu Hospital of Shandong University, Jinan 250012, ChinaKey Laboratory of Chemical Biology of Natural Products (Ministry of Education), School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, ChinaKey Laboratory of Chemical Biology of Natural Products (Ministry of Education), School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, ChinaKey Laboratory of Chemical Biology of Natural Products (Ministry of Education), School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, ChinaKey Laboratory of Chemical Biology of Natural Products (Ministry of Education), School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, ChinaKey Laboratory of Chemical Biology of Natural Products (Ministry of Education), School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, ChinaKey Laboratory of Chemical Biology of Natural Products (Ministry of Education), School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, ChinaKey Laboratory of Chemical Biology of Natural Products (Ministry of Education), School of Pharmaceutical Sciences, Cheeloo College of Medicine, Shandong University, Jinan 250012, ChinaLiverworts are rich in bibenzyls and related <i>O</i>-glycosides, which show antioxidant activity. However, glycosyltransferases that catalyze the glycosylation of bibenzyls have not yet been characterized. Here, we identified two bibenzyl UDP-glucosyltransferases named <i>Mp</i>UGT737B1 and <i>Mp</i>UGT741A1 from the model liverwort <i>Marchantia polymorpha</i>. The in vitro enzymatic assay revealed that <i>Mp</i>UGT741A1 specifically accepted the bibenzyl lunularin as substrate. <i>Mp</i>UGT737B1 could accept bibenzyls, dihydrochalcone and phenylpropanoids as substrates, and could convert phloretin to phloretin-4-<i>O</i>-glucoside and phloridzin, which showed inhibitory activity against tyrosinase and antioxidant activity. The results of sugar donor selectivity showed that <i>Mp</i>UGT737B1 and <i>Mp</i>UGT741A1 could only accept UDP-glucose as a substrate. The expression levels of these <i>Mp</i>UGTs were considerably increased after UV irradiation, which generally caused oxidative damage. This result indicates that <i>Mp</i>UGT737B1 and <i>Mp</i>UGT741A1 may play a role in plant stress adaption. Subcellular localization indicates that <i>Mp</i>UGT737B1 and <i>Mp</i>UGT741A1 were expressed in the cytoplasm and nucleus. These enzymes should provide candidate genes for the synthesis of bioactive bibenzyl <i>O</i>-glucosides and the improvement of plant antioxidant capacity.https://www.mdpi.com/2076-3921/11/4/735<i>Marchantia polymorpha</i><i>O</i>-glucosyltransferasebibenzylsbiosynthesisenzymatic catalysis |
| spellingShingle | Rui-Lin Xiong Jiao-Zhen Zhang Xin-Yan Liu Jian-Qun Deng Ting-Ting Zhu Rong Ni Hui Tan Ju-Zheng Sheng Hong-Xiang Lou Ai-Xia Cheng Identification and Characterization of Two Bibenzyl Glycosyltransferases from the Liverwort <i>Marchantia polymorpha</i> Antioxidants <i>Marchantia polymorpha</i> <i>O</i>-glucosyltransferase bibenzyls biosynthesis enzymatic catalysis |
| title | Identification and Characterization of Two Bibenzyl Glycosyltransferases from the Liverwort <i>Marchantia polymorpha</i> |
| title_full | Identification and Characterization of Two Bibenzyl Glycosyltransferases from the Liverwort <i>Marchantia polymorpha</i> |
| title_fullStr | Identification and Characterization of Two Bibenzyl Glycosyltransferases from the Liverwort <i>Marchantia polymorpha</i> |
| title_full_unstemmed | Identification and Characterization of Two Bibenzyl Glycosyltransferases from the Liverwort <i>Marchantia polymorpha</i> |
| title_short | Identification and Characterization of Two Bibenzyl Glycosyltransferases from the Liverwort <i>Marchantia polymorpha</i> |
| title_sort | identification and characterization of two bibenzyl glycosyltransferases from the liverwort i marchantia polymorpha i |
| topic | <i>Marchantia polymorpha</i> <i>O</i>-glucosyltransferase bibenzyls biosynthesis enzymatic catalysis |
| url | https://www.mdpi.com/2076-3921/11/4/735 |
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