IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v446y2007i7134d10.1038_nature05611.html
   My bibliography  Save this article

BluB cannibalizes flavin to form the lower ligand of vitamin B12

Author

Listed:
  • Michiko E. Taga

    (Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA)

  • Nicholas A. Larsen

    (Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA)

  • Annaleise R. Howard-Jones

    (Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA)

  • Christopher T. Walsh

    (Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA)

  • Graham C. Walker

    (Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA)

Abstract

The long road to vitamin B12 Vitamin B12 (cobalamin) is one of the largest known non-polymeric natural products, and it is the only vitamin that is synthesized exclusively by microorganisms. Despite years of study, the biosynthesis of one part of the vitamin is poorly understood. Now the last unknown step in its biosynthesis is revealed. The X-ray crystal structure of BluB, an enzyme that uses molecular oxygen to cleave a flavin mononucleotide cofactor to form the lower ligand of vitamin B12, has been determined. This reaction is an example of an unusual process, the enzymatic destruction of one cofactor to synthesize another.

Suggested Citation

  • Michiko E. Taga & Nicholas A. Larsen & Annaleise R. Howard-Jones & Christopher T. Walsh & Graham C. Walker, 2007. "BluB cannibalizes flavin to form the lower ligand of vitamin B12," Nature, Nature, vol. 446(7134), pages 449-453, March.
    • Handle: RePEc:nat:nature:v:446:y:2007:i:7134:d:10.1038_nature05611
    DOI: 10.1038/nature05611
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature05611
    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/nature05611?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.

    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:446:y:2007:i:7134:d:10.1038_nature05611. 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.