The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases

Kristian E H Frandsen; Thomas J Simmons; Paul Dupree; Jens-Christian N Poulsen; Glyn R Hemsworth; Luisa Ciano; Esther M Johnston; Morten Tovborg; Katja S Johansen; Pernille von Freiesleben; Laurence Marmuse; Sébastien Fort; Sylvain Cottaz; Hugues Driguez; Bernard Henrissat; Nicolas Lenfant; Floriana Tuna; Amgalanbaatar Baldansuren; Gideon J Davies; Leila Lo Leggio; Paul H Walton

doi:10.1038/nchembio.2029

The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases

Kristian E H Frandsen, Thomas J Simmons, Paul Dupree, Jens-Christian N Poulsen, Glyn R Hemsworth, Luisa Ciano, Esther M Johnston, Morten Tovborg, Katja S Johansen, Pernille von Freiesleben, Laurence Marmuse, Sébastien Fort, Sylvain Cottaz, Hugues Driguez, Bernard Henrissat, Nicolas Lenfant, Floriana Tuna, Amgalanbaatar Baldansuren, Gideon J Davies, Leila Lo LeggioPaul H Walton

Research output: Contribution to journal › Article › peer-review

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that oxidatively break down recalcitrant polysaccharides such as cellulose and chitin. Since their discovery, LPMOs have become integral factors in the industrial utilization of biomass, especially in the sustainable generation of cellulosic bioethanol. We report here a structural determination of an LPMO-oligosaccharide complex, yielding detailed insights into the mechanism of action of these enzymes. Using a combination of structure and electron paramagnetic resonance spectroscopy, we reveal the means by which LPMOs interact with saccharide substrates. We further uncover electronic and structural features of the enzyme active site, showing how LPMOs orchestrate the reaction of oxygen with polysaccharide chains.

Original language	English
Pages (from-to)	298-303
Number of pages	6
Journal	Nature chemical biology
Volume	12
Issue number	4
Early online date	29 Feb 2016
DOIs	https://doi.org/10.1038/nchembio.2029
Publication status	Published - Apr 2016

Keywords

Amino Acid Sequence
Aspergillus oryzae
Binding Sites
Catalytic Domain
Cellulose
Chitin
Copper
Crystallography, X-Ray
Fluorescence Resonance Energy Transfer
Lentinula
Mixed Function Oxygenases
Models, Molecular
Molecular Sequence Data
Oligosaccharides
Oxidation-Reduction
Substrate Specificity
Journal Article
Research Support, Non-U.S. Gov't

Access to Document

10.1038/nchembio.2029

Cite this

Frandsen, K. E. H., Simmons, T. J., Dupree, P., Poulsen, J-C. N., Hemsworth, G. R., Ciano, L., Johnston, E. M., Tovborg, M., Johansen, K. S., von Freiesleben, P., Marmuse, L., Fort, S., Cottaz, S., Driguez, H., Henrissat, B., Lenfant, N., Tuna, F., Baldansuren, A., Davies, G. J., ... Walton, P. H. (2016). The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases. Nature chemical biology, 12(4), 298-303. https://doi.org/10.1038/nchembio.2029

@article{e295d19b0ec34762b086dfc24b025452,

title = "The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases",

abstract = "Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that oxidatively break down recalcitrant polysaccharides such as cellulose and chitin. Since their discovery, LPMOs have become integral factors in the industrial utilization of biomass, especially in the sustainable generation of cellulosic bioethanol. We report here a structural determination of an LPMO-oligosaccharide complex, yielding detailed insights into the mechanism of action of these enzymes. Using a combination of structure and electron paramagnetic resonance spectroscopy, we reveal the means by which LPMOs interact with saccharide substrates. We further uncover electronic and structural features of the enzyme active site, showing how LPMOs orchestrate the reaction of oxygen with polysaccharide chains.",

keywords = "Amino Acid Sequence, Aspergillus oryzae, Binding Sites, Catalytic Domain, Cellulose, Chitin, Copper, Crystallography, X-Ray, Fluorescence Resonance Energy Transfer, Lentinula, Mixed Function Oxygenases, Models, Molecular, Molecular Sequence Data, Oligosaccharides, Oxidation-Reduction, Substrate Specificity, Journal Article, Research Support, Non-U.S. Gov't",

author = "Frandsen, {Kristian E H} and Simmons, {Thomas J} and Paul Dupree and Poulsen, {Jens-Christian N} and Hemsworth, {Glyn R} and Luisa Ciano and Johnston, {Esther M} and Morten Tovborg and Johansen, {Katja S} and {von Freiesleben}, Pernille and Laurence Marmuse and S{\'e}bastien Fort and Sylvain Cottaz and Hugues Driguez and Bernard Henrissat and Nicolas Lenfant and Floriana Tuna and Amgalanbaatar Baldansuren and Davies, {Gideon J} and {Lo Leggio}, Leila and Walton, {Paul H}",

year = "2016",

month = apr,

doi = "10.1038/nchembio.2029",

language = "English",

volume = "12",

pages = "298--303",

journal = "Nature chemical biology",

issn = "1552-4450",

publisher = "Springer Nature",

number = "4",

}

Frandsen, KEH, Simmons, TJ, Dupree, P, Poulsen, J-CN, Hemsworth, GR, Ciano, L, Johnston, EM, Tovborg, M, Johansen, KS, von Freiesleben, P, Marmuse, L, Fort, S, Cottaz, S, Driguez, H, Henrissat, B, Lenfant, N, Tuna, F, Baldansuren, A, Davies, GJ, Lo Leggio, L & Walton, PH 2016, 'The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases', Nature chemical biology, vol. 12, no. 4, pp. 298-303. https://doi.org/10.1038/nchembio.2029

TY - JOUR

T1 - The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases

AU - Frandsen, Kristian E H

AU - Simmons, Thomas J

AU - Dupree, Paul

AU - Poulsen, Jens-Christian N

AU - Hemsworth, Glyn R

AU - Ciano, Luisa

AU - Johnston, Esther M

AU - Tovborg, Morten

AU - Johansen, Katja S

AU - von Freiesleben, Pernille

AU - Marmuse, Laurence

AU - Fort, Sébastien

AU - Cottaz, Sylvain

AU - Driguez, Hugues

AU - Henrissat, Bernard

AU - Lenfant, Nicolas

AU - Tuna, Floriana

AU - Baldansuren, Amgalanbaatar

AU - Davies, Gideon J

AU - Lo Leggio, Leila

AU - Walton, Paul H

PY - 2016/4

Y1 - 2016/4

N2 - Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that oxidatively break down recalcitrant polysaccharides such as cellulose and chitin. Since their discovery, LPMOs have become integral factors in the industrial utilization of biomass, especially in the sustainable generation of cellulosic bioethanol. We report here a structural determination of an LPMO-oligosaccharide complex, yielding detailed insights into the mechanism of action of these enzymes. Using a combination of structure and electron paramagnetic resonance spectroscopy, we reveal the means by which LPMOs interact with saccharide substrates. We further uncover electronic and structural features of the enzyme active site, showing how LPMOs orchestrate the reaction of oxygen with polysaccharide chains.

AB - Lytic polysaccharide monooxygenases (LPMOs) are copper-containing enzymes that oxidatively break down recalcitrant polysaccharides such as cellulose and chitin. Since their discovery, LPMOs have become integral factors in the industrial utilization of biomass, especially in the sustainable generation of cellulosic bioethanol. We report here a structural determination of an LPMO-oligosaccharide complex, yielding detailed insights into the mechanism of action of these enzymes. Using a combination of structure and electron paramagnetic resonance spectroscopy, we reveal the means by which LPMOs interact with saccharide substrates. We further uncover electronic and structural features of the enzyme active site, showing how LPMOs orchestrate the reaction of oxygen with polysaccharide chains.

KW - Amino Acid Sequence

KW - Aspergillus oryzae

KW - Binding Sites

KW - Catalytic Domain

KW - Cellulose

KW - Chitin

KW - Copper

KW - Crystallography, X-Ray

KW - Fluorescence Resonance Energy Transfer

KW - Lentinula

KW - Mixed Function Oxygenases

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Oligosaccharides

KW - Oxidation-Reduction

KW - Substrate Specificity

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1038/nchembio.2029

DO - 10.1038/nchembio.2029

M3 - Article

C2 - 26928935

SN - 1552-4450

VL - 12

SP - 298

EP - 303

JO - Nature chemical biology

JF - Nature chemical biology

IS - 4

ER -

The molecular basis of polysaccharide cleavage by lytic polysaccharide monooxygenases

Abstract

Keywords

Access to Document

Fingerprint

Cite this