KIB OpenIR
A 2-oxoglutarate-dependent dioxygenase converts dihydrofuran to furan in Salvia diterpenoids
Song,Jiao-Jiao; Fang,Xin; Li,Chen-Yi; Jiang,Yan; Li,Jian-Xu; Wu,Sheng; Guo,Juan; Liu,Yan; Fan,Hang; Huang,Yan-Bo; Wei,Yu-Kun; Kong,Yu; Zhao,Qing; Xu,Jing-Jing; Hu,Yong-Hong; Chen,Xiao-Ya; Yang,Lei
2022
Source PublicationPLANT PHYSIOLOGY
ISSN0032-0889
Volume188Issue:3Pages:1496-1506
AbstractA 2-oxoglutarate-dependent dioxygenase is responsible for tanshinone IIA biosynthesis in medicinal herb Salvia miltiorrhiza, which controls the metabolite flux from dihydrofuran- to furan-tanshinones.Tanshinone IIA (TIIA), a diterpene quinone with a furan ring, is a bioactive compound found in the medicinal herb redroot sage (Salvia miltiorrhiza Bunge), in which both furan and dihydrofuran analogs are present in abundance. Progress has been made recently in elucidating the tanshinone biosynthetic pathway, including heterocyclization of the dihydrofuran D-ring by cytochrome P450s; however, dehydrogenation of dihydrofuran to furan, a key step of furan ring formation, remains uncharacterized. Here, by differential transcriptome mining, we identified six 2-oxoglutarate-dependent dioxygenase (2-ODD) genes whose expressions corresponded to tanshinone biosynthesis. We showed that Sm2-ODD14 acts as a dehydrogenase catalyzing the furan ring aromatization. In vitro Sm2-ODD14 converted cryptotanshinone to TIIA and thus was designated TIIA synthase (SmTIIAS). Furthermore, SmTIIAS showed a strict substrate specificity, and repression of SmTIIAS expression in hairy root by RNAi led to increased accumulation of total dihydrofuran-tanshinones and decreased production of furan-tanshinones. We conclude that SmTIIAS controls the metabolite flux from dihydrofuran- to furan-tanshinones, which influences medicinal properties of S. miltiorrhiza.
KeywordMOLECULAR-CLONING BIOSYNTHESIS TANSHINONES EVOLUTION CYTOTOXICITY SUPERFAMILY OXYGENASES APOPTOSIS SYNTHASE
DOI10.1093/plphys/kiab567
WOS IDWOS:000764825700001
Citation statistics
Cited Times:41[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.kib.ac.cn/handle/151853/73159
Collection中国科学院昆明植物研究所
Affiliation1.Shanghai Chenshan Bot Garden, Shanghai Key Lab Plant Funct Genom & Resources, Shanghai 201602, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Chinese Acad Sci, Kunming Inst Bot, State Key Lab Phytochem & Plant Resources West Ch, Kunming 650201, Yunnan, Peoples R China
4.Chinese Acad Sci, CAS Ctr Excellence Mol Plant Sci, State Key Lab Plant Mol Genet, Shanghai Inst Plant Physiol & Ecol, Shanghai 200032, Peoples R China
5.Shanghai Normal Univ, Sch Life Sci, Shanghai 200234, Peoples R China
6.Univ Calif Riverside, Dept Chem & Environm Engn, Riverside, CA 92521 USA
7.China Acad Chinese Med Sci, Natl Resource Ctr Chinese Mat Med, State Key Lab Dao Di Herbs, Beijing 100700, Peoples R China
Recommended Citation
GB/T 7714
Song,Jiao-Jiao,Fang,Xin,Li,Chen-Yi,et al. A 2-oxoglutarate-dependent dioxygenase converts dihydrofuran to furan in Salvia diterpenoids[J]. PLANT PHYSIOLOGY,2022,188(3):1496-1506.
APA Song,Jiao-Jiao.,Fang,Xin.,Li,Chen-Yi.,Jiang,Yan.,Li,Jian-Xu.,...&Yang,Lei.(2022).A 2-oxoglutarate-dependent dioxygenase converts dihydrofuran to furan in Salvia diterpenoids.PLANT PHYSIOLOGY,188(3),1496-1506.
MLA Song,Jiao-Jiao,et al."A 2-oxoglutarate-dependent dioxygenase converts dihydrofuran to furan in Salvia diterpenoids".PLANT PHYSIOLOGY 188.3(2022):1496-1506.
Files in This Item:
There are no files associated with this item.
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Song,Jiao-Jiao]'s Articles
[Fang,Xin]'s Articles
[Li,Chen-Yi]'s Articles
Baidu academic
Similar articles in Baidu academic
[Song,Jiao-Jiao]'s Articles
[Fang,Xin]'s Articles
[Li,Chen-Yi]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Song,Jiao-Jiao]'s Articles
[Fang,Xin]'s Articles
[Li,Chen-Yi]'s Articles
Terms of Use
No data!
Social Bookmark/Share
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.