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.
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Acknowledgements
We thank V. Chechik and J. Guo-Wang for assistance with EPR measurements and R. Gregory and J. Robinson for laboratory assistance. This work was funded by the Biotechnology and Biological Sciences Research Council (BB/I014802/1). We thank Diamond Light Source for access to beamlines.
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G.R.H. and P.H.W. performed laboratory experiments; B.H. did the sequence analysis; and G.J.D., B.H., G.R.H. and P.H.W. wrote the paper.
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Supplementary Results, Supplementary Figures 1–6 and Supplementary Tables 1–3. (PDF 1580 kb)
Supplementary Data Set 1
Sequences that were retrieved with significant e-values using BAE61530 as the query for a BLAST search against the non-redundant protein sequence database of the NCBI (PDF 484 kb)
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Hemsworth, G., Henrissat, B., Davies, G. et al. Discovery and characterization of a new family of lytic polysaccharide monooxygenases. Nat Chem Biol 10, 122–126 (2014). https://doi.org/10.1038/nchembio.1417
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DOI: https://doi.org/10.1038/nchembio.1417
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