4.8 Article

A 2-oxoglutarate-dependent dioxygenase converts dihydrofuran to furan in Salvia diterpenoids

Journal

PLANT PHYSIOLOGY
Volume 188, Issue 3, Pages 1496-1506

Publisher

OXFORD UNIV PRESS INC
DOI: 10.1093/plphys/kiab567

Keywords

-

Categories

Funding

  1. National Key R&D Program of China [2020YFA0907900]
  2. National Natural Science Foundation of China [32070338, 31900255]
  3. International Partnership Program of Chinese Academy of Sciences [153D31KYSB20160074]
  4. Strategic Biological Resources and Technology Supporting System from the Chinese Academy of Sciences [ZSZY-001]
  5. Special Fund for Shanghai Landscaping Administration Bureau Program [G192419, G222414]

Ask authors/readers for more resources

A 2-oxoglutarate-dependent dioxygenase (2-ODD) gene responsible for tanshinone IIA biosynthesis in Salvia miltiorrhiza was identified in this study. The gene, known as Sm2-ODD14, acts as a dehydrogenase and catalyzes the aromatization of the furan ring. The study also showed that Sm2-ODD14 controls the metabolite flux from dihydrofuran- to furan-tanshinones, which impacts the medicinal properties of S. miltiorrhiza.
A 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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.8
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available