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

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*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Article number5961
Number of pages9
JournalNature Communications
Publication statusPublished - 22 Jan 2015

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

Cite this