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Functional Characterization of a Flavonoid Glycosyltransferase in Sweet Orange (Citrus sinensis)
Fruits of sweet orange (Citrus sinensis), a popular commercial Citrus species, contain high concentrations of flavonoids beneficial to human health. These fruits predominantly accumulate O-glycosylated flavonoids, in which the disaccharides [neohesperidose (rhamnosyl-α-1,2-glucose) or rutinose (rham...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Frontiers Media S.A.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5818429/ https://www.ncbi.nlm.nih.gov/pubmed/29497429 http://dx.doi.org/10.3389/fpls.2018.00166 |
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author | Liu, Xiaogang Lin, Cailing Ma, Xiaodi Tan, Yan Wang, Jiuzhao Zeng, Ming |
author_facet | Liu, Xiaogang Lin, Cailing Ma, Xiaodi Tan, Yan Wang, Jiuzhao Zeng, Ming |
author_sort | Liu, Xiaogang |
collection | PubMed |
description | Fruits of sweet orange (Citrus sinensis), a popular commercial Citrus species, contain high concentrations of flavonoids beneficial to human health. These fruits predominantly accumulate O-glycosylated flavonoids, in which the disaccharides [neohesperidose (rhamnosyl-α-1,2-glucose) or rutinose (rhamnosyl-α-1,6-glucose)] are linked to the flavonoid aglycones through the 3- or 7-hydroxyl sites. The biotransformation of the flavonoid aglycones into O-rutinosides or O-neohesperidosides in the Citrus plants usually consists of two glycosylation reactions involving a series of uridine diphosphate-sugar dependent glycosyltransferases (UGTs). Although several genes encoding flavonoid UGTs have been functionally characterized in the Citrus plants, full elucidation of the flavonoid glycosylation process remains elusive. Based on the available genomic and transcriptome data, we isolated a UGT with a high expression level in the sweet orange fruits that possibly encodes a flavonoid glucosyltransferase and/or rhamnosyltransferase. Biochemical analyses revealed that a broad range of flavonoid substrates could be glucosylated at their 3- and/or 7-hydrogen sites by the recombinant enzyme, including hesperetin, naringenin, diosmetin, quercetin, and kaempferol. Furthermore, overexpression of the gene could significantly increase the accumulations of quercetin 7-O-rhamnoside, quercetin 7-O-glucoside, and kaempferol 7-O-glucoside, implying that the enzyme has flavonoid 7-O-glucosyltransferase and 7-O-rhamnosyltransferase activities in vivo. |
format | Online Article Text |
id | pubmed-5818429 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-58184292018-03-01 Functional Characterization of a Flavonoid Glycosyltransferase in Sweet Orange (Citrus sinensis) Liu, Xiaogang Lin, Cailing Ma, Xiaodi Tan, Yan Wang, Jiuzhao Zeng, Ming Front Plant Sci Plant Science Fruits of sweet orange (Citrus sinensis), a popular commercial Citrus species, contain high concentrations of flavonoids beneficial to human health. These fruits predominantly accumulate O-glycosylated flavonoids, in which the disaccharides [neohesperidose (rhamnosyl-α-1,2-glucose) or rutinose (rhamnosyl-α-1,6-glucose)] are linked to the flavonoid aglycones through the 3- or 7-hydroxyl sites. The biotransformation of the flavonoid aglycones into O-rutinosides or O-neohesperidosides in the Citrus plants usually consists of two glycosylation reactions involving a series of uridine diphosphate-sugar dependent glycosyltransferases (UGTs). Although several genes encoding flavonoid UGTs have been functionally characterized in the Citrus plants, full elucidation of the flavonoid glycosylation process remains elusive. Based on the available genomic and transcriptome data, we isolated a UGT with a high expression level in the sweet orange fruits that possibly encodes a flavonoid glucosyltransferase and/or rhamnosyltransferase. Biochemical analyses revealed that a broad range of flavonoid substrates could be glucosylated at their 3- and/or 7-hydrogen sites by the recombinant enzyme, including hesperetin, naringenin, diosmetin, quercetin, and kaempferol. Furthermore, overexpression of the gene could significantly increase the accumulations of quercetin 7-O-rhamnoside, quercetin 7-O-glucoside, and kaempferol 7-O-glucoside, implying that the enzyme has flavonoid 7-O-glucosyltransferase and 7-O-rhamnosyltransferase activities in vivo. Frontiers Media S.A. 2018-02-15 /pmc/articles/PMC5818429/ /pubmed/29497429 http://dx.doi.org/10.3389/fpls.2018.00166 Text en Copyright © 2018 Liu, Lin, Ma, Tan, Wang and Zeng. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Plant Science Liu, Xiaogang Lin, Cailing Ma, Xiaodi Tan, Yan Wang, Jiuzhao Zeng, Ming Functional Characterization of a Flavonoid Glycosyltransferase in Sweet Orange (Citrus sinensis) |
title | Functional Characterization of a Flavonoid Glycosyltransferase in Sweet Orange (Citrus sinensis) |
title_full | Functional Characterization of a Flavonoid Glycosyltransferase in Sweet Orange (Citrus sinensis) |
title_fullStr | Functional Characterization of a Flavonoid Glycosyltransferase in Sweet Orange (Citrus sinensis) |
title_full_unstemmed | Functional Characterization of a Flavonoid Glycosyltransferase in Sweet Orange (Citrus sinensis) |
title_short | Functional Characterization of a Flavonoid Glycosyltransferase in Sweet Orange (Citrus sinensis) |
title_sort | functional characterization of a flavonoid glycosyltransferase in sweet orange (citrus sinensis) |
topic | Plant Science |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5818429/ https://www.ncbi.nlm.nih.gov/pubmed/29497429 http://dx.doi.org/10.3389/fpls.2018.00166 |
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