Two residues determine the product profile of the class II diterpene synthases TPS14 and TPS21 of Tripterygium wilfordii

Hansen, Nikolaj L.; Nissen, Jakob N.; Hamberger, Björn

doi:10.1016/j.phytochem.2017.02.022

Title: Two residues determine the product profile of the class II diterpene synthases TPS14 and TPS21 of Tripterygium wilfordii

Full Record
Other Related Research

Authors:: Hansen, Nikolaj L.; Nissen, Jakob N.; Hamberger, Björn

Publication Date:: 2017-06-01

Sponsoring Org.:: USDOE

OSTI Identifier:: 1413527

Grant/Contract Number:: BER DE-FC02-07ER64494

Resource Type:: Publisher's Accepted Manuscript

Journal Name:: Phytochemistry

Additional Journal Information:: Journal Name: Phytochemistry Journal Volume: 138 Journal Issue: C; Journal ID: ISSN 0031-9422

Publisher:: Elsevier

Country of Publication:: United Kingdom

Language:: English

Citation Formats


                    Hansen, Nikolaj L., Nissen, Jakob N., and Hamberger, Björn. Two residues determine the product profile of the class II diterpene synthases TPS14 and TPS21 of Tripterygium wilfordii.  United Kingdom: N. p., 2017. 
Web.  doi:10.1016/j.phytochem.2017.02.022.

Copy to clipboard


                    Hansen, Nikolaj L., Nissen, Jakob N., & Hamberger, Björn. Two residues determine the product profile of the class II diterpene synthases TPS14 and TPS21 of Tripterygium wilfordii.  United Kingdom.  https://doi.org/10.1016/j.phytochem.2017.02.022

Copy to clipboard


                    Hansen, Nikolaj L., Nissen, Jakob N., and Hamberger, Björn. Thu .  
"Two residues determine the product profile of the class II diterpene synthases TPS14 and TPS21 of Tripterygium wilfordii".  United Kingdom.  https://doi.org/10.1016/j.phytochem.2017.02.022.

Copy to clipboard


                    
@article{osti_1413527,

  title        = {Two residues determine the product profile of the class II diterpene synthases TPS14 and TPS21 of Tripterygium wilfordii},

  author       = {Hansen, Nikolaj L. and Nissen, Jakob N. and Hamberger, Björn},

  abstractNote = {},

  doi          = {10.1016/j.phytochem.2017.02.022},

  journal      = {Phytochemistry},

  number       = C,

  volume       = 138,

  place        = {United Kingdom},

  year         = {2017},

  month        = {6}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Accepted Manuscript (Publisher)

Publisher's Version of Record
https://doi.org/10.1016/j.phytochem.2017.02.022

Other availability

Search WorldCat to find libraries that may hold this journal

Citation Metrics:

Cited by: 6 works

Citation information provided by
Web of Science

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

Two residues determine the product profile of the class II diterpene synthases TPS14 and TPS21 of Tripterygium wilfordii

Journal Article Hansen, Nikolaj L. ; Nissen, Jakob N. ; Hamberger, Björn - Phytochemistry

Not provided.
https://doi.org/10.1016/j.phytochem.2017.02.022
The terpene synthase gene family in Tripterygium wilfordii harbors a labdane-type diterpene synthase among the monoterpene synthase TPS-b subfamily

Journal Article Hansen, Nikolaj L. ; Heskes, Allison M. ; Hamberger, Britta ; ... - The Plant Journal

We present Tripterygium wilfordii (Celastraceae) is a medicinal plant with anti-inflammatory and immunosuppressive properties. Identification of a vast array of unusual sesquiterpenoids, diterpenoids and triterpenoids in T. wilfordii has spurred investigations of their pharmacological properties. The tri-epoxide lactone triptolide was the first of many diterpenoids identified, attracting interest due to the spectrum of bioactivities. To probe the genetic underpinning of diterpenoid diversity, an expansion of the class II diterpene synthase (diTPS) family was recently identified in a leaf transcriptome. Following detection of triptolide and simple diterpene scaffolds in the root, we sequenced and mined the root transcriptome. This allowed identificationmore »« less
Cited by 24
https://doi.org/10.1111/tpj.13410

Full Text Available
Novosphingobium aromaticivorans uses a Nu-class glutathione S-transferase as a glutathione lyase in breaking the β-aryl ether bond of lignin

Journal Article Kontur, Wayne S. ; Bingman, Craig A. ; Olmsted, Charles N. ; ... - Journal of Biological Chemistry

As a major component of plant cells walls, lignin is a potential renewable source of valuable chemicals. Several sphingomonad bacteria have been identified that can break the β-aryl ether bond connecting most phenylpropanoid units of the lignin heteropolymer. Here, we tested three sphingomonads predicted to be capable of breaking the β-aryl ether bond of the dimeric aromatic compound guaiacylglycerol-β-guaiacyl ether (GGE) and found that Novosphingobium aromaticivorans metabolizes GGE at one of the fastest rates thus far reported. After the ether bond of racemic GGE is broken by replacement with a thioether bond involving glutathione, the glutathione moiety must be removedmore »« less
Cited by 5
https://doi.org/10.1074/jbc.RA117.001268
Higher-order oligomerization of a chimeric αβγ bifunctional diterpene synthase with prenyltransferase and class II cyclase activities is concentration-dependent

Journal Article Ronnebaum, T ; Gupta, K. ; Christianson, D. - Journal of Structural Biology
https://doi.org/10.1016/j.jsb.2020.107463
Higher-order oligomerization of a chimeric αβγ bifunctional diterpene synthase with prenyltransferase and class II cyclase activities is concentration-dependent

Journal Article Ronnebaum, Trey A. ; Gupta, Kushol ; Christianson, David W. - Journal of Structural Biology
https://doi.org/10.1016/j.jsb.2020.107463

Similar Records