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

Kemisk Institut

167 Citationer (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.

Originalsprog	Engelsk
Artikelnummer	5961
Tidsskrift	Nature Communications
Vol/bind	6
Antal sider	9
ISSN	2041-1723
DOI	https://doi.org/10.1038/ncomms6961
Status	Udgivet - 22 jan. 2015

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10.1038/ncomms6961Licens: CC BY

Leggio_2015_Structure_and_boostingForlagets udgivne version, 1,53 MBLicens: CC BY

Citationsformater

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

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, bind 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.",

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

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

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

C2 - 25608804

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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