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Investigating the Catalytic Activity of Glycosyltransferase on Quercetin from Tripterygium wilfordii
[Image: see text] Flavonoid glycosides have shown many pharmacological activities in clinical studies. However, the main way to obtain flavonoid glycosides is to extract and separate them from plants, which wastes both time and resources. Here, we identified the O-glycosyltransferase (UGTs) TwUGT3 f...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical
Society
2020
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6990443/ https://www.ncbi.nlm.nih.gov/pubmed/32010813 http://dx.doi.org/10.1021/acsomega.9b02919 |
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author | Gao, Jie Ma, Baowei Lu, Yun Zhang, Yifeng Tong, Yuru Guo, Siyuan Gao, Wei Huang, Luqi |
author_facet | Gao, Jie Ma, Baowei Lu, Yun Zhang, Yifeng Tong, Yuru Guo, Siyuan Gao, Wei Huang, Luqi |
author_sort | Gao, Jie |
collection | PubMed |
description | [Image: see text] Flavonoid glycosides have shown many pharmacological activities in clinical studies. However, the main way to obtain flavonoid glycosides is to extract and separate them from plants, which wastes both time and resources. Here, we identified the O-glycosyltransferase (UGTs) TwUGT3 from Tripterygium wilfordii and analyzed its bioinformatics. First, the enzyme was found to utilize phloretin and uridine diphosphate glucose (UDPG) as substrates to produce an acid-tolerant glucoside. Then, it also can use quercetin and UDPG as substrates to produce the corresponding O-glucoside. In addition, we further explored the substrate specificity of TwUGT3, which suggested that it also accepts luteolin, pinocembrin, and genistein to produce the corresponding O-glucosides. Subsequently, the optimum pH, reaction time, reaction temperature, and enzymatic kinetic parameters of TwUGT3 were determined. |
format | Online Article Text |
id | pubmed-6990443 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | American Chemical
Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-69904432020-01-31 Investigating the Catalytic Activity of Glycosyltransferase on Quercetin from Tripterygium wilfordii Gao, Jie Ma, Baowei Lu, Yun Zhang, Yifeng Tong, Yuru Guo, Siyuan Gao, Wei Huang, Luqi ACS Omega [Image: see text] Flavonoid glycosides have shown many pharmacological activities in clinical studies. However, the main way to obtain flavonoid glycosides is to extract and separate them from plants, which wastes both time and resources. Here, we identified the O-glycosyltransferase (UGTs) TwUGT3 from Tripterygium wilfordii and analyzed its bioinformatics. First, the enzyme was found to utilize phloretin and uridine diphosphate glucose (UDPG) as substrates to produce an acid-tolerant glucoside. Then, it also can use quercetin and UDPG as substrates to produce the corresponding O-glucoside. In addition, we further explored the substrate specificity of TwUGT3, which suggested that it also accepts luteolin, pinocembrin, and genistein to produce the corresponding O-glucosides. Subsequently, the optimum pH, reaction time, reaction temperature, and enzymatic kinetic parameters of TwUGT3 were determined. American Chemical Society 2020-01-13 /pmc/articles/PMC6990443/ /pubmed/32010813 http://dx.doi.org/10.1021/acsomega.9b02919 Text en Copyright © 2020 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes. |
spellingShingle | Gao, Jie Ma, Baowei Lu, Yun Zhang, Yifeng Tong, Yuru Guo, Siyuan Gao, Wei Huang, Luqi Investigating the Catalytic Activity of Glycosyltransferase on Quercetin from Tripterygium wilfordii |
title | Investigating the
Catalytic Activity of Glycosyltransferase on Quercetin from Tripterygium wilfordii |
title_full | Investigating the
Catalytic Activity of Glycosyltransferase on Quercetin from Tripterygium wilfordii |
title_fullStr | Investigating the
Catalytic Activity of Glycosyltransferase on Quercetin from Tripterygium wilfordii |
title_full_unstemmed | Investigating the
Catalytic Activity of Glycosyltransferase on Quercetin from Tripterygium wilfordii |
title_short | Investigating the
Catalytic Activity of Glycosyltransferase on Quercetin from Tripterygium wilfordii |
title_sort | investigating the
catalytic activity of glycosyltransferase on quercetin from tripterygium wilfordii |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6990443/ https://www.ncbi.nlm.nih.gov/pubmed/32010813 http://dx.doi.org/10.1021/acsomega.9b02919 |
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