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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...
Autores principales: | , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Pub. Group
2015
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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. |
format | Online Article Text |
id | pubmed-4338556 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Nature Pub. Group |
record_format | MEDLINE/PubMed |
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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