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Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase

Author

Listed:
  • Leila Lo Leggio

    (University of Copenhagen)

  • Thomas J. Simmons

    (University Of Cambridge)

  • Jens-Christian N. Poulsen

    (University of Copenhagen)

  • Kristian E. H. Frandsen

    (University of Copenhagen)

  • Glyn R. Hemsworth

    (University of York)

  • Mary A. Stringer

    (Novozymes A/S, Krogshoejvej 36)

  • Pernille von Freiesleben

    (Novozymes A/S, Krogshoejvej 36)

  • Morten Tovborg

    (Novozymes A/S, Krogshoejvej 36)

  • Katja S. Johansen

    (Novozymes A/S, Krogshoejvej 36)

  • Leonardo De Maria

    (Novozymes A/S, Krogshoejvej 36
    Present address: Novo Nordisk, Diabetes Structural Biology, Novo Nordisk Park, 2760 Maaloev, Denmark)

  • Paul V. Harris

    (Novozymes, Inc., 1445 Drew Avenue)

  • Chee-Leong Soong

    (Novozymes North America Inc.)

  • Paul Dupree

    (University Of Cambridge)

  • Theodora Tryfona

    (University Of Cambridge)

  • Nicolas Lenfant

    (Architecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université)

  • Bernard Henrissat

    (Architecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université
    King Abdulaziz University)

  • Gideon J. Davies

    (University of York)

  • Paul H. Walton

    (University of York)

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are recently discovered enzymes that oxidatively deconstruct polysaccharides. LPMOs are fundamental in the effective utilization of these substrates by bacteria and fungi; moreover, the enzymes have significant industrial importance. We report here the activity, spectroscopy and three-dimensional structure of a starch-active LPMO, a representative of the new CAZy AA13 family. We demonstrate that these enzymes generate aldonic acid-terminated malto-oligosaccharides from retrograded starch and boost significantly the conversion of this recalcitrant substrate to maltose by β-amylase. The detailed structure of the enzyme’s active site yields insights into the mechanism of action of this important class of enzymes.

Suggested Citation

  • Leila Lo Leggio & Thomas J. Simmons & Jens-Christian N. Poulsen & Kristian E. H. Frandsen & Glyn R. Hemsworth & Mary A. Stringer & Pernille von Freiesleben & Morten Tovborg & Katja S. Johansen & Leona, 2015. "Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase," Nature Communications, Nature, vol. 6(1), pages 1-9, May.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms6961
    DOI: 10.1038/ncomms6961
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    Cited by:

    1. Tanveer S. Batth & Jonas L. Simonsen & Cristina Hernández-Rollán & Søren Brander & Jens Preben Morth & Katja S. Johansen & Morten H. H. Nørholm & Jakob B. Hoof & Jesper V. Olsen, 2023. "A seven-transmembrane methyltransferase catalysing N-terminal histidine methylation of lytic polysaccharide monooxygenases," Nature Communications, Nature, vol. 14(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.
    3. Usmani, Zeba & Sharma, Minaxi & Awasthi, Abhishek Kumar & Lukk, Tiit & Tuohy, Maria G. & Gong, Liang & Nguyen-Tri, Phuong & Goddard, Alan D. & Bill, Roslyn M. & Nayak, S.Chandra & Gupta, Vijai Kumar, 2021. "Lignocellulosic biorefineries: The current state of challenges and strategies for efficient commercialization," Renewable and Sustainable Energy Reviews, Elsevier, vol. 148(C).

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