IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v11y2020i1d10.1038_s41467-020-19561-8.html
   My bibliography  Save this article

Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)

Author

Listed:
  • Riin Kont

    (University of Tartu)

  • Bastien Bissaro

    (NMBU—Norwegian University of Life Sciences
    INRAE, Aix Marseille University, UMR1163 Biodiversité et Biotechnologie Fongiques)

  • Vincent G. H. Eijsink

    (NMBU—Norwegian University of Life Sciences)

  • Priit Väljamäe

    (University of Tartu)

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are widely distributed in Nature, where they catalyze the hydroxylation of glycosidic bonds in polysaccharides. Despite the importance of LPMOs in the global carbon cycle and in industrial biomass conversion, the catalytic properties of these monocopper enzymes remain enigmatic. Strikingly, there is a remarkable lack of kinetic data, likely due to a multitude of experimental challenges related to the insoluble nature of LPMO substrates, like cellulose and chitin, and to the occurrence of multiple side reactions. Here, we employed competition between well characterized reference enzymes and LPMOs for the H2O2 co-substrate to kinetically characterize LPMO-catalyzed cellulose oxidation. LPMOs of both bacterial and fungal origin showed high peroxygenase efficiencies, with kcat/KmH2O2 values in the order of 105–106 M−1 s−1. Besides providing crucial insight into the cellulolytic peroxygenase reaction, these results show that LPMOs belonging to multiple families and active on multiple substrates are true peroxygenases.

Suggested Citation

  • Riin Kont & Bastien Bissaro & Vincent G. H. Eijsink & Priit Väljamäe, 2020. "Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)," Nature Communications, Nature, vol. 11(1), pages 1-10, December.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19561-8
    DOI: 10.1038/s41467-020-19561-8
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-020-19561-8
    File Function: Abstract
    Download Restriction: no

    File URL: https://libkey.io/10.1038/s41467-020-19561-8?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
    ---><---

    Citations

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


    Cited by:

    1. Iván Ayuso-Fernández & Tom Z. Emrich-Mills & Julia Haak & Ole Golten & Kelsi R. Hall & Lorenz Schwaiger & Trond S. Moe & Anton A. Stepnov & Roland Ludwig & George E. Cutsail III & Morten Sørlie & Åsmu, 2024. "Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO)," Nature Communications, Nature, vol. 15(1), pages 1-15, December.
    2. Hucheng Chang & Neus Gacias Amengual & Alexander Botz & Lorenz Schwaiger & Daniel Kracher & Stefan Scheiblbrandner & Florian Csarman & Roland Ludwig, 2022. "Investigating lytic polysaccharide monooxygenase-assisted wood cell wall degradation with microsensors," 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:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-19561-8. 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.