Researchers from the University of York (UK) and Aix-Marseille Université (France) have discovered a new family of enzymes that can degrade hard-to-digest biomass into its constituent sugars. They report on the new family of lytic polysaccharide monooxygenases in a paper in the journal Nature Chemical Biology.
Lytic polysaccharide monooxygenases (LPMOs) constitute a recently discovered class of enzymes that have attracted 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.
The new paper reports the discovery of a third.
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.—Hemsworth et al.
The research at York was funded by the Biotechnology and Biological Sciences Research Council (BBSRC).
Glyn R Hemsworth, Bernard Henrissat, Gideon J Davies & Paul H Walton (2013) “Discovery and characterization of a new family of lytic polysaccharide monooxygenases.” Nature Chemical Biology doi: 10.1038/nchembio.1417