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UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius
OBJECTIVE: In order to obtain new glycosyltransferases with highly efficient catalysis, the glycosyltransferases from Carthamus tinctorius which contains diverse types of glycosides were mined. Methods: A new glycosyltransferase gene (UGT88B2) with full length was obtained by PCR and further transfo...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9476720/ https://www.ncbi.nlm.nih.gov/pubmed/36120177 http://dx.doi.org/10.1016/j.chmed.2020.05.010 |
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author | Sui, Song-yang Guo, Rui-mingqian Xie, Ke-bo Yang, Lin Dai, Jun-gui |
author_facet | Sui, Song-yang Guo, Rui-mingqian Xie, Ke-bo Yang, Lin Dai, Jun-gui |
author_sort | Sui, Song-yang |
collection | PubMed |
description | OBJECTIVE: In order to obtain new glycosyltransferases with highly efficient catalysis, the glycosyltransferases from Carthamus tinctorius which contains diverse types of glycosides were mined. Methods: A new glycosyltransferase gene (UGT88B2) with full length was obtained by PCR and further transformed into Escherichia coli for heterologous expression. The catalytic activity of recombinant UGT88B2 was determined by HPLC-MS(n). The structures of representative catalytic products were elucidated by MS and NMR. RESULTS: UGT88B2 exhibited catalytic promiscuity and various patterns in glycosylation of flavonoids with high efficiency. CONCLUSION: A new glycosyltransferase named UGT88B2 was successfully mined and can be employed as enzymatic tools in glycosylation of flavonoids. |
format | Online Article Text |
id | pubmed-9476720 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
spelling | pubmed-94767202022-09-16 UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius Sui, Song-yang Guo, Rui-mingqian Xie, Ke-bo Yang, Lin Dai, Jun-gui Chin Herb Med Original Article OBJECTIVE: In order to obtain new glycosyltransferases with highly efficient catalysis, the glycosyltransferases from Carthamus tinctorius which contains diverse types of glycosides were mined. Methods: A new glycosyltransferase gene (UGT88B2) with full length was obtained by PCR and further transformed into Escherichia coli for heterologous expression. The catalytic activity of recombinant UGT88B2 was determined by HPLC-MS(n). The structures of representative catalytic products were elucidated by MS and NMR. RESULTS: UGT88B2 exhibited catalytic promiscuity and various patterns in glycosylation of flavonoids with high efficiency. CONCLUSION: A new glycosyltransferase named UGT88B2 was successfully mined and can be employed as enzymatic tools in glycosylation of flavonoids. Elsevier 2020-09-18 /pmc/articles/PMC9476720/ /pubmed/36120177 http://dx.doi.org/10.1016/j.chmed.2020.05.010 Text en © 2020 Tianjin Press of Chinese Herbal Medicines. Published by ELSEVIER B.V. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/). |
spellingShingle | Original Article Sui, Song-yang Guo, Rui-mingqian Xie, Ke-bo Yang, Lin Dai, Jun-gui UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius |
title | UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius |
title_full | UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius |
title_fullStr | UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius |
title_full_unstemmed | UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius |
title_short | UGT88B2: A promiscuous O-glycosyltransferase from Carthamus tinctorius |
title_sort | ugt88b2: a promiscuous o-glycosyltransferase from carthamus tinctorius |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9476720/ https://www.ncbi.nlm.nih.gov/pubmed/36120177 http://dx.doi.org/10.1016/j.chmed.2020.05.010 |
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