IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v483y2012i7389d10.1038_nature10865.html
   My bibliography  Save this article

Enzymatic catalysis of anti-Baldwin ring closure in polyether biosynthesis

Author

Listed:
  • Kinya Hotta

    (National University of Singapore, 14 Science Drive 4, 117543 Singapore)

  • Xi Chen

    (National University of Singapore, 14 Science Drive 4, 117543 Singapore)

  • Robert S. Paton

    (Chemistry Research Laboratory, University of Oxford, Mansfield Road, Oxford OX1 3TA, UK)

  • Atsushi Minami

    (Hokkaido University, Graduate School of Science, North 10 West 8, Sapporo 060-0810, Japan)

  • Hao Li

    (National University of Singapore, 14 Science Drive 4, 117543 Singapore)

  • Kunchithapadam Swaminathan

    (National University of Singapore, 14 Science Drive 4, 117543 Singapore)

  • Irimpan I. Mathews

    (Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, 2575 Sand Hill Road MS 99, Menlo Park, California 95124, USA)

  • Kenji Watanabe

    (University of Shizuoka, Graduate School of Pharmaceutical Sciences, 52-1 Yada, Suruga-ku, Shizuoka City, Shizuoka 422-8526, Japan)

  • Hideaki Oikawa

    (Hokkaido University, Graduate School of Science, North 10 West 8, Sapporo 060-0810, Japan)

  • Kendall N. Houk

    (University of California Los Angeles, 607 Charles E. Young Drive East, Box 951569, Los Angeles, California 90095-1569, USA)

  • Chu-Young Kim

    (National University of Singapore, 14 Science Drive 4, 117543 Singapore)

Abstract

The X-ray crystal structure of the epoxide hydrolase Lsd19 in complex with its substrate and product analogue is determined, providing insight into a general mechanism of enzyme-catalysed formation of polyether natural products.

Suggested Citation

  • Kinya Hotta & Xi Chen & Robert S. Paton & Atsushi Minami & Hao Li & Kunchithapadam Swaminathan & Irimpan I. Mathews & Kenji Watanabe & Hideaki Oikawa & Kendall N. Houk & Chu-Young Kim, 2012. "Enzymatic catalysis of anti-Baldwin ring closure in polyether biosynthesis," Nature, Nature, vol. 483(7389), pages 355-358, March.
  • Handle: RePEc:nat:nature:v:483:y:2012:i:7389:d:10.1038_nature10865
    DOI: 10.1038/nature10865
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature10865
    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/nature10865?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. Qian Wang & Ning Liu & Yaming Deng & Yuze Guan & Hongli Xiao & Tara A. Nitka & Hui Yang & Anju Yadav & Lela Vukovic & Irimpan I. Mathews & Xi Chen & Chu-Young Kim, 2023. "Triepoxide formation by a flavin-dependent monooxygenase in monensin biosynthesis," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    2. Jun-Kuan Li & Ge Qu & Xu Li & Yuchen Tian & Chengsen Cui & Fa-Guang Zhang & Wuyuan Zhang & Jun-An Ma & Manfred T. Reetz & Zhoutong Sun, 2022. "Rational enzyme design for enabling biocatalytic Baldwin cyclization and asymmetric synthesis of chiral heterocycles," Nature Communications, Nature, vol. 13(1), pages 1-11, 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:483:y:2012:i:7389:d:10.1038_nature10865. 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.