Production of salidroside in metabolically engineered Escherichia coli

Salidroside (1) is the most important bioactive component of Rhodiola (also called as “Tibetan Ginseng”), which is a valuable medicinal herb exhibiting several adaptogenic properties. Due to the inefficiency of plant extraction and chemical synthesis, the supply of salidroside (1) is currently limit...

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Main Authors:	Bai, Yanfen, Bi, Huiping, Zhuang, Yibin, Liu, Chang, Cai, Tao, Liu, Xiaonan, Zhang, Xueli, Liu, Tao, Ma, Yanhe
Format:	Online
Language:	English
Published:	Nature Publishing Group 2014
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4200411/

id	pubmed-4200411
recordtype	oai_dc
spelling	pubmed-42004112014-10-21 Production of salidroside in metabolically engineered Escherichia coli Bai, Yanfen Bi, Huiping Zhuang, Yibin Liu, Chang Cai, Tao Liu, Xiaonan Zhang, Xueli Liu, Tao Ma, Yanhe Article Salidroside (1) is the most important bioactive component of Rhodiola (also called as “Tibetan Ginseng”), which is a valuable medicinal herb exhibiting several adaptogenic properties. Due to the inefficiency of plant extraction and chemical synthesis, the supply of salidroside (1) is currently limited. Herein, we achieved unprecedented biosynthesis of salidroside (1) from glucose in a microorganism. First, the pyruvate decarboxylase ARO10 and endogenous alcohol dehydrogenases were recruited to convert 4-hydroxyphenylpyruvate (2), an intermediate of L-tyrosine pathway, to tyrosol (3) in Escherichia coli. Subsequently, tyrosol production was improved by overexpressing the pathway genes, and by eliminating competing pathways and feedback inhibition. Finally, by introducing Rhodiola-derived glycosyltransferase UGT73B6 into the above-mentioned recombinant strain, salidroside (1) was produced with a titer of 56.9 mg/L. Interestingly, the Rhodiola-derived glycosyltransferase, UGT73B6, also catalyzed the attachment of glucose to the phenol position of tyrosol (3) to form icariside D2 (4), which was not reported in any previous literatures. Nature Publishing Group 2014-10-17 /pmc/articles/PMC4200411/ /pubmed/25323006 http://dx.doi.org/10.1038/srep06640 Text en Copyright © 2014, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-sa/4.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder in order to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/4.0/
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Bai, Yanfen Bi, Huiping Zhuang, Yibin Liu, Chang Cai, Tao Liu, Xiaonan Zhang, Xueli Liu, Tao Ma, Yanhe
spellingShingle	Bai, Yanfen Bi, Huiping Zhuang, Yibin Liu, Chang Cai, Tao Liu, Xiaonan Zhang, Xueli Liu, Tao Ma, Yanhe Production of salidroside in metabolically engineered Escherichia coli
author_facet	Bai, Yanfen Bi, Huiping Zhuang, Yibin Liu, Chang Cai, Tao Liu, Xiaonan Zhang, Xueli Liu, Tao Ma, Yanhe
author_sort	Bai, Yanfen
title	Production of salidroside in metabolically engineered Escherichia coli
title_short	Production of salidroside in metabolically engineered Escherichia coli
title_full	Production of salidroside in metabolically engineered Escherichia coli
title_fullStr	Production of salidroside in metabolically engineered Escherichia coli
title_full_unstemmed	Production of salidroside in metabolically engineered Escherichia coli
title_sort	production of salidroside in metabolically engineered escherichia coli
description	Salidroside (1) is the most important bioactive component of Rhodiola (also called as “Tibetan Ginseng”), which is a valuable medicinal herb exhibiting several adaptogenic properties. Due to the inefficiency of plant extraction and chemical synthesis, the supply of salidroside (1) is currently limited. Herein, we achieved unprecedented biosynthesis of salidroside (1) from glucose in a microorganism. First, the pyruvate decarboxylase ARO10 and endogenous alcohol dehydrogenases were recruited to convert 4-hydroxyphenylpyruvate (2), an intermediate of L-tyrosine pathway, to tyrosol (3) in Escherichia coli. Subsequently, tyrosol production was improved by overexpressing the pathway genes, and by eliminating competing pathways and feedback inhibition. Finally, by introducing Rhodiola-derived glycosyltransferase UGT73B6 into the above-mentioned recombinant strain, salidroside (1) was produced with a titer of 56.9 mg/L. Interestingly, the Rhodiola-derived glycosyltransferase, UGT73B6, also catalyzed the attachment of glucose to the phenol position of tyrosol (3) to form icariside D2 (4), which was not reported in any previous literatures.
publisher	Nature Publishing Group
publishDate	2014
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4200411/
_version_	1613145922316795904

Production of salidroside in metabolically engineered Escherichia coli

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