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

Research output: Contribution to journal › Journal article › Research › peer-review

253 Citations (Scopus)

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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 - 2015

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Leggio_2015_Structure_and_boostingFinal published version, 1.53 MBLicence: CC BY

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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, [5961]. https://doi.org/10.1038/ncomms6961

Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase. / Lo Leggio, Leila; Simmons, Thomas J.; Poulsen, Jens-Christian Navarro ; Frandsen, Kristian Erik Høpfner; Hemsworth, Glyn R.; Stringer, Mary A.; von Freiesleben, Pernille; Tovborg, Morten; Johansen, Katja Salomon; De Maria, Leonardo; Harris, Paul V.; Soong, Chee-Leong; Dupree, Paul; Tryfona, Theodora; Lenfant, Nicolas; Henrissat, Bernard; Davies, Gideon J.; Walton, Paul H.

In: Nature Communications, Vol. 6, 5961, 2015.

Research output: Contribution to journal › Journal article › Research › peer-review

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

Lo Leggio, Leila ; Simmons, Thomas J. ; Poulsen, Jens-Christian Navarro ; Frandsen, Kristian Erik Høpfner ; Hemsworth, Glyn R. ; Stringer, Mary A. ; von Freiesleben, Pernille ; Tovborg, Morten ; Johansen, Katja Salomon ; De Maria, Leonardo ; Harris, Paul V. ; Soong, Chee-Leong ; Dupree, Paul ; Tryfona, Theodora ; Lenfant, Nicolas ; Henrissat, Bernard ; Davies, Gideon J. ; Walton, Paul H. / Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase. In: Nature Communications. 2015 ; Vol. 6.

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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

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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

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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

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JO - Nature Communications

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