Discovery and characterization of a new family of lytic polysaccharide monooxygenases

Discovery and characterization of a new family of lytic polysaccharide monooxygenases Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of enzymes capable of oxidizing recalcitrant polysaccharides. They are attracting considerable attention owing to their potential use in biomass conversion, notably in the production of biofuels. Previous studies have identified two discrete sequence-based families of these enzymes termed AA9 (formerly GH61) and AA10 (formerly CBM33). Here, we report the discovery of a third family of LPMOs. Using a chitin-degrading exemplar from Aspergillus oryzae , we show that the three-dimensional structure of the enzyme shares some features of the previous two classes of LPMOs, including a copper active center featuring the 'histidine brace' active site, but is distinct in terms of its active site details and its EPR spectroscopy. The newly characterized AA11 family expands the LPMO clan, potentially broadening both the range of potential substrates and the types of reactive copper-oxygen species formed at the active site of LPMOs. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Chemical Biology Nature Publishing Group (NPG)

Discovery and characterization of a new family of lytic polysaccharide monooxygenases

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Publisher
Nature Publishing Group (NPG)
Copyright
Copyright © 2013 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.
ISSN
1552-4450
eISSN
1552-4469
D.O.I.
10.1038/nchembio.1417
Publisher site
See Article on Publisher Site

Abstract

Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of enzymes capable of oxidizing recalcitrant polysaccharides. They are attracting considerable attention owing to their potential use in biomass conversion, notably in the production of biofuels. Previous studies have identified two discrete sequence-based families of these enzymes termed AA9 (formerly GH61) and AA10 (formerly CBM33). Here, we report the discovery of a third family of LPMOs. Using a chitin-degrading exemplar from Aspergillus oryzae , we show that the three-dimensional structure of the enzyme shares some features of the previous two classes of LPMOs, including a copper active center featuring the 'histidine brace' active site, but is distinct in terms of its active site details and its EPR spectroscopy. The newly characterized AA11 family expands the LPMO clan, potentially broadening both the range of potential substrates and the types of reactive copper-oxygen species formed at the active site of LPMOs.

Journal

Nature Chemical BiologyNature Publishing Group (NPG)

Published: Dec 22, 2013

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