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

Leila Lo Leggio (1) , Thomas J. Simmons (2) , Jens-Christian N. Poulsen (1) , Kristian E. H. Frandsen (1) , Glyn R. Hemsworth (3) , Mary A. Stringer (4) , Pernille Von Freiesleben (4) , Morten Tovborg (4) , Katja S. Johansen (4) , Leonardo de Maria (4) , Paul V. Harris (4) , Chee-Leong Soong (4) , Paul Dupree (2) , Theodora Tryfona (2) , Nicolas Lenfant (5) , Bernard Henrissat (5) , Gideon J. Davies (3) , Paul H. Walton (3)

1 ITU - IT University of Copenhagen
2 CAM - University of Cambridge [UK]
3 University of York [York, UK]
4 Novozymes
5 AFMB - Architecture et fonction des macromolécules biologiques

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.

Mots clés: Biotechnology; Structural biology

Domaines: Biologie structurale [q-bio.BM]; Bio-Informatique, Biologie Systémique [q-bio.QM]

Leila Lo Leggio, Thomas J. Simmons, Jens-Christian N. Poulsen, Kristian E. H. Frandsen, Glyn R. Hemsworth, et al.. Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase. Nature Communications, 2015, 6, pp.5961. ⟨10.1038/ncomms6961⟩. ⟨hal-01439010⟩