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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...

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Detalles Bibliográficos
Autores principales: Sui, Song-yang, Guo, Rui-mingqian, Xie, Ke-bo, Yang, Lin, Dai, Jun-gui
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2020
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.
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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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