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

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Dokumenter

Leila Lo Leggio, Thomas J. Simmons, Jens-Christian Navarro Poulsen, Kristian Erik Høpfner Frandsen, Glyn R. Hemsworth, Mary A. Stringer, Pernille von Freiesleben, Morten Tovborg, Katja Salomon Johansen, Leonardo De Maria, Paul V. Harris, Chee-Leong Soong, Paul Dupree, Theodora Tryfona, Nicolas Lenfant, Bernard Henrissat, Gideon J. Davies, Paul H. Walton

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.

OriginalsprogEngelsk
Artikelnummer5961
TidsskriftNature Communications
Vol/bind6
Antal sider9
ISSN2041-1723
DOI
StatusUdgivet - 2015

Antal downloads er baseret på statistik fra Google Scholar og www.ku.dk


Ingen data tilgængelig

ID: 130691568