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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-01-22

AUTHORS

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

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. More... »

PAGES

5961

Journal

TITLE

Nature Communications

ISSUE

1

VOLUME

6

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/ncomms6961

DOI

http://dx.doi.org/10.1038/ncomms6961

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1012380337

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/25608804


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