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

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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.

I: Nature Communications, Bind 6, 5961, 2015.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

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

APA

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

Vancouver

Lo Leggio L, Simmons TJ, Poulsen J-CN, Frandsen KEH, Hemsworth GR, Stringer MA o.a. Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase. Nature Communications. 2015;6. 5961. https://doi.org/10.1038/ncomms6961

Author

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. I: Nature Communications. 2015 ; Bind 6.

Bibtex

@article{eda3de9cbe76470491b6120c1940e0df,
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.}",
year = "2015",
doi = "10.1038/ncomms6961",
language = "English",
volume = "6",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

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 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

Y1 - 2015

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

VL - 6

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 5961

ER -

ID: 130691568