IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v469y2011i7328d10.1038_nature09628.html
   My bibliography  Save this article

Taxadiene synthase structure and evolution of modular architecture in terpene biosynthesis

Author

Listed:
  • Mustafa Köksal

    (Roy and Diana Vagelos Laboratories, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, USA)

  • Yinghua Jin

    (University of Illinois at Urbana-Champaign
    University of Colorado)

  • Robert M. Coates

    (University of Illinois at Urbana-Champaign)

  • Rodney Croteau

    (Institute of Biological Chemistry, Washington State University)

  • David W. Christianson

    (Roy and Diana Vagelos Laboratories, University of Pennsylvania, 231 South 34th Street, Philadelphia, Pennsylvania 19104-6323, USA)

Abstract

Taxol-synthesizing enzyme structure The first step in the biosynthesis of the anticancer compound Taxol (paclitaxel) and many other natural C20 diterpenes is the cyclization of an isoprenoid, catalysed by taxadiene synthase. The X-ray crystal structure of this enzyme from the Pacific yew has now been determined. Its C-terminal catalytic domain binds and activates the substrate in a manner seen in class I terpenoid cyclases, but the N-terminal domain and a third 'insertion' domain adopt the fold of a class II terpenoid cyclase. This suggests that this enzyme could be the ancestral progenitor of all terpenoid cyclases.

Suggested Citation

  • Mustafa Köksal & Yinghua Jin & Robert M. Coates & Rodney Croteau & David W. Christianson, 2011. "Taxadiene synthase structure and evolution of modular architecture in terpene biosynthesis," Nature, Nature, vol. 469(7328), pages 116-120, January.
    • Handle: RePEc:nat:nature:v:469:y:2011:i:7328:d:10.1038_nature09628
    DOI: 10.1038/nature09628
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature09628
    File Function: Abstract
    Download Restriction: Access to the full text of the articles in this series is restricted.
    File URL: https://libkey.io/10.1038/nature09628?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    As the access to this document is restricted, you may want to search for a different version of it.

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Zhong Li & Lilan Zhang & Kangwei Xu & Yuanyuan Jiang & Jieke Du & Xingwang Zhang & Ling-Hong Meng & Qile Wu & Lei Du & Xiaoju Li & Yuechan Hu & Zhenzhen Xie & Xukai Jiang & Ya-Jie Tang & Ruibo Wu & Re, 2023. "Molecular insights into the catalytic promiscuity of a bacterial diterpene synthase," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:nature:v:469:y:2011:i:7328:d:10.1038_nature09628. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.