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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...

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Autores principales: Gao, Jie, Ma, Baowei, Lu, Yun, Zhang, Yifeng, Tong, Yuru, Guo, Siyuan, Gao, Wei, Huang, Luqi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
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.
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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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