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Characterization of a bifunctional O- and N-glucosyltransferase from Vitis vinifera in glucosylating phenolic compounds and 3,4-dichloroaniline in Pichia pastoris and Arabidopsis thaliana.


ABSTRACT: 2,4,5-Trichlorophenol, 2,6-dimethylphenol, 3-methylcatechol, phenol, hydroquinone, catechol, and 3,4-dichloroaniline are present in the environment and are risky to humans and animals because of their wide applications in many industries. In this study, a putative uridine diphosphate glucose-dependent glycosyltransferase from Vitis vinifera (VvUGT72B1) displayed high O-glucosyltransferase or N-glucosyltransferase activity toward all these xenbiotics and was able to enhance the resistance of P. pastoris to them. Compared with wild-type Arabidopsis plants, VvUGT72B1-transgenic Arabidopsis plants showed higher resistance to all the xenobiotics except for phenol and exhibited higher removal efficiencies against all xenobiotics. Glucosides of 3-methylcatechol, 2,6-dimethylphenol, phenol, and 3,4-dichloroaniline were exported to the surrounding media by Arabidopsis plants while transgenic Arabidopsis plants exported more glucosides than wild-type Arabidopsis plants. Our findings have the potential to provide a broader spectrum remediation strategy for the phytoremoval and degradation of phenolic compounds and 3,4-dichloroaniline than previous works.

SUBMITTER: Xu ZS 

PROVIDER: S-EPMC3828253 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Characterization of a bifunctional O- and N-glucosyltransferase from Vitis vinifera in glucosylating phenolic compounds and 3,4-dichloroaniline in Pichia pastoris and Arabidopsis thaliana.

Xu Zhi-Sheng ZS   Xue Wei W   Xiong Ai-Sheng AS   Lin Ya-Qiu YQ   Xu Jing J   Zhu Bo B   Zhao Wei W   Peng Ri-He RH   Yao Quan-Hong QH  

PloS one 20131114 11


2,4,5-Trichlorophenol, 2,6-dimethylphenol, 3-methylcatechol, phenol, hydroquinone, catechol, and 3,4-dichloroaniline are present in the environment and are risky to humans and animals because of their wide applications in many industries. In this study, a putative uridine diphosphate glucose-dependent glycosyltransferase from Vitis vinifera (VvUGT72B1) displayed high O-glucosyltransferase or N-glucosyltransferase activity toward all these xenbiotics and was able to enhance the resistance of P. p  ...[more]

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