IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v503y2013i7477d10.1038_nature12643.html
   My bibliography  Save this article

Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement

Author

Listed:
  • Robin Teufel

    (Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego)

  • Akimasa Miyanaga

    (Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego)

  • Quentin Michaudel

    (The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA)

  • Frederick Stull

    (Program in Chemical Biology, University of Michigan)

  • Gordon Louie

    (Howard Hughes Medical Institute, The Salk Institute for Biological Studies, Jack H. Skirball Center for Chemical Biology and Proteomics)

  • Joseph P. Noel

    (Howard Hughes Medical Institute, The Salk Institute for Biological Studies, Jack H. Skirball Center for Chemical Biology and Proteomics)

  • Phil S. Baran

    (The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037, USA)

  • Bruce Palfey

    (Program in Chemical Biology, University of Michigan
    University of Michigan)

  • Bradley S. Moore

    (Center for Marine Biotechnology and Biomedicine, Scripps Institution of Oceanography, University of California San Diego
    Skaggs School of Pharmacy and Pharmaceutical Sciences, University of California San Diego)

Abstract

Structural and functional studies reveal how the bacterial flavoenzyme EncM catalyses the oxygenation–dehydrogenation dual oxidation of a highly reactive substrate, and show that EncM maintains a stable flavin oxygenating species that promotes substrate oxidation and triggers a rarely seen Favorskii-type rearrangement.

Suggested Citation

  • Robin Teufel & Akimasa Miyanaga & Quentin Michaudel & Frederick Stull & Gordon Louie & Joseph P. Noel & Phil S. Baran & Bruce Palfey & Bradley S. Moore, 2013. "Flavin-mediated dual oxidation controls an enzymatic Favorskii-type rearrangement," Nature, Nature, vol. 503(7477), pages 552-556, November.
    • Handle: RePEc:nat:nature:v:503:y:2013:i:7477:d:10.1038_nature12643
    DOI: 10.1038/nature12643
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature12643
    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/nature12643?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. Ke-Na Feng & Yue Zhang & Mingfang Zhang & Yan-Long Yang & Ji-Kai Liu & Lifeng Pan & Ying Zeng, 2023. "A flavin-monooxygenase catalyzing oxepinone formation and the complete biosynthesis of vibralactone," Nature Communications, Nature, vol. 14(1), pages 1-13, 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:503:y:2013:i:7477:d:10.1038_nature12643. 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.