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

TY - JOUR

T1 - Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase

AU - Lo Leggio, Leila

AU - Simmons, Thomas J.

AU - Poulsen, Jens Christian N

AU - Frandsen, Kristian E H

AU - Hemsworth, Glyn R.

AU - Stringer, Mary A.

AU - Von Freiesleben, Pernille

AU - Tovborg, Morten

AU - Johansen, Katja S.

AU - De Maria, Leonardo

AU - Harris, Paul V.

AU - Soong, Chee Leong

AU - Dupree, Paul

AU - Tryfona, Theodora

AU - Lenfant, Nicolas

AU - Henrissat, Bernard

AU - Davies, Gideon J.

AU - Walton, Paul H.

N1 - © 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 http://creativecommons.org/licenses/by/4.0/

PY - 2015/1/22

Y1 - 2015/1/22

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84955324784&partnerID=8YFLogxK

U2 - 10.1038/ncomms6961

DO - 10.1038/ncomms6961

M3 - Article

C2 - 25608804

SN - 2041-1723

VL - 6

JO - Nature Communications

JF - Nature Communications

M1 - 5961

ER -