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

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

doi:10.1038/ncomms6961

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

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

Department of Chemistry

167 Citations (Scopus)

131 Downloads (Pure)

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.

Original language	English
Article number	5961
Journal	Nature Communications
Volume	6
Number of pages	9
ISSN	2041-1723
DOIs	https://doi.org/10.1038/ncomms6961
Publication status	Published - 22 Jan 2015

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Lo Leggio, L., Simmons, T. J., Poulsen, J.-C. N., Frandsen, K. E. H., Hemsworth, G. R., Stringer, M. A., von Freiesleben, P., Tovborg, M., Johansen, K. S., De Maria, L., Harris, P. V., Soong, C.-L., Dupree, P., Tryfona, T., Lenfant, N., Henrissat, B., Davies, G. J., & Walton, P. H. (2015). Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase. Nature Communications, 6, Article 5961. https://doi.org/10.1038/ncomms6961

Lo Leggio, L, Simmons, TJ, Poulsen, J-CN , Frandsen, KEH, Hemsworth, GR, Stringer, MA, von Freiesleben, P, Tovborg, M, Johansen, KS, De Maria, L, Harris, PV, Soong, C-L, Dupree, P, Tryfona, T, Lenfant, N, Henrissat, B, Davies, GJ & Walton, PH 2015, 'Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase', Nature Communications, vol. 6, 5961. https://doi.org/10.1038/ncomms6961

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title = "Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase",

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.",

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AU - Lo Leggio, Leila

AU - Simmons, Thomas J.

AU - Poulsen, Jens-Christian Navarro

AU - Frandsen, Kristian Erik Høpfner

AU - Hemsworth, Glyn R.

AU - Stringer, Mary A.

AU - von Freiesleben, Pernille

AU - Tovborg, Morten

AU - Johansen, Katja Salomon

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.

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 enzyme's 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 enzyme's active site yields insights into the mechanism of action of this important class of enzymes.

U2 - 10.1038/ncomms6961

DO - 10.1038/ncomms6961

M3 - Journal article

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SN - 2041-1723

VL - 6

JO - Nature Communications

JF - Nature Communications

M1 - 5961

ER -

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

Abstract

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