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From the same journal

From the same journal

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

Research output: Contribution to journalArticle


  • 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
  • Leonardo De Maria
  • Paul V. Harris
  • Chee Leong Soong
  • Paul Dupree
  • Theodora Tryfona
  • Nicolas Lenfant
  • Bernard Henrissat
  • Gideon J. Davies
  • Paul H. Walton


Publication details

JournalNature Communications
DateAccepted/In press - 25 Nov 2014
DatePublished (current) - 22 Jan 2015
Number of pages9
Original languageEnglish


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 enzymes active site yields insights into the mechanism of action of this important class of enzymes.

Bibliographical note

© 2015 Macmillan Publishers Limited. This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line. To view a copy of this license, visit


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