Biochemical and in silico characterization of glycosyltransferases from red sweet cherry (Prunus avium L.) reveals their broad specificity toward phenolic substrates
Polyphenolic compounds are a class of phytonutrients that play important roles in plants and contribute to human health when incorporated into our diet through fruit consumption. A large proportion occur as glycoconjugates but the enzymes responsible for their glycosylation are poorly characterized....
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| Format: | Article |
| Language: | English |
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Elsevier
2024-07-01
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| Series: | Food Chemistry: Molecular Sciences |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2666566223000333 |
| _version_ | 1797356088304074752 |
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| author | Daniel Clayton-Cuch Long Yu Daniel McDougal Crista A. Burbidge John B. Bruning David Bradley Christine Böttcher Vincent Bulone |
| author_facet | Daniel Clayton-Cuch Long Yu Daniel McDougal Crista A. Burbidge John B. Bruning David Bradley Christine Böttcher Vincent Bulone |
| author_sort | Daniel Clayton-Cuch |
| collection | DOAJ |
| description | Polyphenolic compounds are a class of phytonutrients that play important roles in plants and contribute to human health when incorporated into our diet through fruit consumption. A large proportion occur as glycoconjugates but the enzymes responsible for their glycosylation are poorly characterized. Here, we report the biochemical and structural characterization of two glycosyltransferases from sweet cherry named PaUGT1 and PaUGT2. Both are promiscuous glucosyltransferases active on diverse anthocyanidins and flavonols, as well as phenolic acids in the case of PaUGT1. They also exhibit weaker galactosyltransferase activity. The expression of the gene encoding PaUGT1, the most active of the two proteins, follows anthocyanin accumulation during fruit ripening, suggesting that this enzyme is the primary glycosyltransferase involved in flavonoid glycosylation in sweet cherry. It can potentially be used to synthesize diverse glycoconjugates of flavonoids for integration into bioactive formulations, and for generating new fruit cultivars with enhanced health-promoting properties using breeding methods. |
| first_indexed | 2024-03-08T14:20:33Z |
| format | Article |
| id | doaj.art-d04020a61e1e47778c5b2c43c0856df5 |
| institution | Directory Open Access Journal |
| issn | 2666-5662 |
| language | English |
| last_indexed | 2024-03-08T14:20:33Z |
| publishDate | 2024-07-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: Molecular Sciences |
| spelling | doaj.art-d04020a61e1e47778c5b2c43c0856df52024-01-14T05:40:14ZengElsevierFood Chemistry: Molecular Sciences2666-56622024-07-018100193Biochemical and in silico characterization of glycosyltransferases from red sweet cherry (Prunus avium L.) reveals their broad specificity toward phenolic substratesDaniel Clayton-Cuch0Long Yu1Daniel McDougal2Crista A. Burbidge3John B. Bruning4David Bradley5Christine Böttcher6Vincent Bulone7Adelaide Glycomics, University of Adelaide, School of Agriculture, Food and Wine, Waite Campus, Adelaide, South Australia 5064, Australia; CSIRO, Waite Campus, Glen Osmond, South Australia 5064, AustraliaAdelaide Glycomics, University of Adelaide, School of Agriculture, Food and Wine, Waite Campus, Adelaide, South Australia 5064, AustraliaInstitute for Photonics and Advanced Sensing (IPAS), School of Biological Sciences, The University of Adelaide, Adelaide, South Australia 5005, AustraliaCSIRO, Waite Campus, Glen Osmond, South Australia 5064, AustraliaInstitute for Photonics and Advanced Sensing (IPAS), School of Biological Sciences, The University of Adelaide, Adelaide, South Australia 5005, AustraliaAgilent Technologies Australia Pty Ltd, Mulgrave, Melbourne, Victoria 3171, AustraliaCSIRO, Waite Campus, Glen Osmond, South Australia 5064, Australia; Corresponding authors at: CSIRO, Waite Campus, Glen Osmond, South Australia 5064, Australia (C. Böttcher), and College of Medicine and Public Health, Flinders University, Bedford Park Campus, Sturt Road, SA 5042, Australia (V. Bulone).Adelaide Glycomics, University of Adelaide, School of Agriculture, Food and Wine, Waite Campus, Adelaide, South Australia 5064, Australia; Division of Glycoscience, Department of Chemistry, School of Engineering Sciences in Chemistry, Biotechnology and Health, Royal Institute of Technology (KTH), AlbaNova University Centre, Stockholm 10691, Sweden; Corresponding authors at: CSIRO, Waite Campus, Glen Osmond, South Australia 5064, Australia (C. Böttcher), and College of Medicine and Public Health, Flinders University, Bedford Park Campus, Sturt Road, SA 5042, Australia (V. Bulone).Polyphenolic compounds are a class of phytonutrients that play important roles in plants and contribute to human health when incorporated into our diet through fruit consumption. A large proportion occur as glycoconjugates but the enzymes responsible for their glycosylation are poorly characterized. Here, we report the biochemical and structural characterization of two glycosyltransferases from sweet cherry named PaUGT1 and PaUGT2. Both are promiscuous glucosyltransferases active on diverse anthocyanidins and flavonols, as well as phenolic acids in the case of PaUGT1. They also exhibit weaker galactosyltransferase activity. The expression of the gene encoding PaUGT1, the most active of the two proteins, follows anthocyanin accumulation during fruit ripening, suggesting that this enzyme is the primary glycosyltransferase involved in flavonoid glycosylation in sweet cherry. It can potentially be used to synthesize diverse glycoconjugates of flavonoids for integration into bioactive formulations, and for generating new fruit cultivars with enhanced health-promoting properties using breeding methods.http://www.sciencedirect.com/science/article/pii/S2666566223000333AnthocyaninsCherryGlycosyltransferaseFlavonolsProtein structure modellingPhenolic compounds |
| spellingShingle | Daniel Clayton-Cuch Long Yu Daniel McDougal Crista A. Burbidge John B. Bruning David Bradley Christine Böttcher Vincent Bulone Biochemical and in silico characterization of glycosyltransferases from red sweet cherry (Prunus avium L.) reveals their broad specificity toward phenolic substrates Food Chemistry: Molecular Sciences Anthocyanins Cherry Glycosyltransferase Flavonols Protein structure modelling Phenolic compounds |
| title | Biochemical and in silico characterization of glycosyltransferases from red sweet cherry (Prunus avium L.) reveals their broad specificity toward phenolic substrates |
| title_full | Biochemical and in silico characterization of glycosyltransferases from red sweet cherry (Prunus avium L.) reveals their broad specificity toward phenolic substrates |
| title_fullStr | Biochemical and in silico characterization of glycosyltransferases from red sweet cherry (Prunus avium L.) reveals their broad specificity toward phenolic substrates |
| title_full_unstemmed | Biochemical and in silico characterization of glycosyltransferases from red sweet cherry (Prunus avium L.) reveals their broad specificity toward phenolic substrates |
| title_short | Biochemical and in silico characterization of glycosyltransferases from red sweet cherry (Prunus avium L.) reveals their broad specificity toward phenolic substrates |
| title_sort | biochemical and in silico characterization of glycosyltransferases from red sweet cherry prunus avium l reveals their broad specificity toward phenolic substrates |
| topic | Anthocyanins Cherry Glycosyltransferase Flavonols Protein structure modelling Phenolic compounds |
| url | http://www.sciencedirect.com/science/article/pii/S2666566223000333 |
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