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 and Paul H. Walton ()
Additional contact information
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
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
Gideon J. Davies: University of York
Paul H. Walton: University of York

Nature Communications, 2015, vol. 6, issue 1, 1-9

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms6961

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