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

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 act...

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Autores principales: Lo Leggio, Leila, Simmons, Thomas J., Poulsen, Jens-Christian N., Frandsen, Kristian E. H., Hemsworth, Glyn R., Stringer, Mary A., von Freiesleben, Pernille, Tovborg, Morten, Johansen, Katja S., De Maria, Leonardo, Harris, Paul V., Soong, Chee-Leong, Dupree, Paul, Tryfona, Theodora, Lenfant, Nicolas, Henrissat, Bernard, Davies, Gideon J., Walton, Paul H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Pub. Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4338556/
https://www.ncbi.nlm.nih.gov/pubmed/25608804
http://dx.doi.org/10.1038/ncomms6961
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author Lo Leggio, Leila
Simmons, Thomas J.
Poulsen, Jens-Christian N.
Frandsen, Kristian E. H.
Hemsworth, Glyn R.
Stringer, Mary A.
von Freiesleben, Pernille
Tovborg, Morten
Johansen, Katja S.
De Maria, Leonardo
Harris, Paul V.
Soong, Chee-Leong
Dupree, Paul
Tryfona, Theodora
Lenfant, Nicolas
Henrissat, Bernard
Davies, Gideon J.
Walton, Paul H.
author_facet Lo Leggio, Leila
Simmons, Thomas J.
Poulsen, Jens-Christian N.
Frandsen, Kristian E. H.
Hemsworth, Glyn R.
Stringer, Mary A.
von Freiesleben, Pernille
Tovborg, Morten
Johansen, Katja S.
De Maria, Leonardo
Harris, Paul V.
Soong, Chee-Leong
Dupree, Paul
Tryfona, Theodora
Lenfant, Nicolas
Henrissat, Bernard
Davies, Gideon J.
Walton, Paul H.
author_sort Lo Leggio, Leila
collection PubMed
description 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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spelling pubmed-43385562015-03-20 Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase Lo Leggio, Leila Simmons, Thomas J. Poulsen, Jens-Christian N. Frandsen, Kristian E. H. Hemsworth, Glyn R. Stringer, Mary A. von Freiesleben, Pernille Tovborg, Morten Johansen, Katja S. De Maria, Leonardo Harris, Paul V. Soong, Chee-Leong Dupree, Paul Tryfona, Theodora Lenfant, Nicolas Henrissat, Bernard Davies, Gideon J. Walton, Paul H. Nat Commun Article 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. Nature Pub. Group 2015-01-22 /pmc/articles/PMC4338556/ /pubmed/25608804 http://dx.doi.org/10.1038/ncomms6961 Text en Copyright © 2015, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by/4.0/ 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; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Lo Leggio, Leila
Simmons, Thomas J.
Poulsen, Jens-Christian N.
Frandsen, Kristian E. H.
Hemsworth, Glyn R.
Stringer, Mary A.
von Freiesleben, Pernille
Tovborg, Morten
Johansen, Katja S.
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
title Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase
title_full Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase
title_fullStr Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase
title_full_unstemmed Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase
title_short Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase
title_sort structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4338556/
https://www.ncbi.nlm.nih.gov/pubmed/25608804
http://dx.doi.org/10.1038/ncomms6961
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