IDEAS home Printed from https://ideas.repec.org/a/nat/nature/v478y2011i7370d10.1038_nature10458.html
   My bibliography  Save this article

Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase

Author

Listed:
  • Juan Du

    (Lehrstuhl für Biochemie, Institut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21)

  • Rafael F. Say

    (Lehrstuhl für Mikrobiologie, Albert-Ludwigs-Universität Freiburg, Schänzlestrasse 1)

  • Wei Lü

    (Lehrstuhl für Biochemie, Institut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21)

  • Georg Fuchs

    (Lehrstuhl für Mikrobiologie, Albert-Ludwigs-Universität Freiburg, Schänzlestrasse 1)

  • Oliver Einsle

    (Lehrstuhl für Biochemie, Institut für organische Chemie und Biochemie, Albert-Ludwigs-Universität Freiburg, Albertstrasse 21
    BIOSS Centre for Biological Signalling Studies, Albert-Ludwigs-Universität Freiburg, Hebelstrasse 25)

Abstract

One active site, two activities The archaeal enzyme fructose 1,6-bisphosphate (FBP) aldolase/phosphatase catalyses two successive reactions in gluconeogenesis: an aldol condensation of dihydroxyacetone phosphate and glyceraldehyde-3-phosphate to form FBP, and its subsequent hydrolysis to fructose-6-phosphate. Two groups present a series of structural snapshots of this novel bifunctional enzyme. The structures reveal a substantial remodelling of the active site that allows it to catalyse two highly dissimilar chemical reactions.

Suggested Citation

  • Juan Du & Rafael F. Say & Wei Lü & Georg Fuchs & Oliver Einsle, 2011. "Active-site remodelling in the bifunctional fructose-1,6-bisphosphate aldolase/phosphatase," Nature, Nature, vol. 478(7370), pages 534-537, October.
  • Handle: RePEc:nat:nature:v:478:y:2011:i:7370:d:10.1038_nature10458
    DOI: 10.1038/nature10458
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/nature10458
    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/nature10458?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. Chongyang Wang & Changshui Liu & Xiaochuan Zhu & Quancai Peng & Qingjun Ma, 2023. "Catalytic site flexibility facilitates the substrate and catalytic promiscuity of Vibrio dual lipase/transferase," Nature Communications, Nature, vol. 14(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:478:y:2011:i:7370:d:10.1038_nature10458. 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.