|
type |
Journal Article |
authors |
Torrens-Spence MP, Pluskal T, Li FS, Carballo V, Weng JK |
title |
Complete Pathway Elucidation and Heterologous Reconstitution of Rhodiola Salidroside Biosynthesis |
journal |
Mol Plant |
Activity |
temporary |
Family |
4.1.1.109.b |
sel |
selected |
ui |
29277428 |
year |
(2018) |
volume |
11 |
number |
1 |
pages |
205-217 |
| |
keywords |
4-hydroxyphenylacetaldehyde; aromatic acetaldehyde synthesis; aromatic amino acid decarboxylase; icariside D2; salidroside; tyrosol |
abstract |
Salidroside is a bioactive tyrosine-derived phenolic natural product found
in medicinal plants under the Rhodiola genus. In addition to their anti-
fatigue and anti-anoxia roles in traditional medicine, Rhodiola total
extract and salidroside have also displayed medicinal properties as anti-
cardiovascular diseases and anti-cancer agents. The resulting surge in
global demand of Rhodiola plants and salidroside has driven some species
close to extinction. Here, we report the full elucidation of the Rhodiola
salidroside biosynthetic pathway utilizing the first comprehensive
transcriptomics and metabolomics datasets for Rhodiola rosea. Unlike the
previously proposed pathway involving separate decarboxylation and
deamination enzymatic steps from tyrosine to the key intermediate 4-
hydroxyphenylacetaldehyde (4-HPAA), Rhodiola contains a pyridoxal phosphate-
dependent 4-HPAA synthase that directly converts tyrosine to 4-HPAA. We
further identified genes encoding the subsequent 4-HPAA reductase and
tyrosol:UDP-glucose 8-O-glucosyltransferase, respectively, to complete
salidroside biosynthesis in Rhodiola. We show that heterologous production
of salidroside can be achieved in the yeast Saccharomyces cerevisiae as well
as the plant Nicotiana benthamiana through transgenic expression of Rhodiola
salidroside biosynthetic genes. This study provides new tools for
engineering sustainable production of salidroside in heterologous hosts. |
last changed |
2019/06/21 13:33 |
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