title: Recent insights into copper-containing lytic polysaccharide mono-oxygenases.
abstract: Recently the role of oxidative enzymes in the degradation of polysaccharides by saprophytic bacteria and fungi was uncovered, challenging the classical model of polysaccharide degradation of being solely via a hydrolytic pathway. 3D structural analyses of lytic polysaccharide mono-oxygenases of both bacterial AA10 (formerly CBM33) and fungal AA9 (formerly GH61) enzymes revealed structures with β-sandwich folds containing an active site with a metal coordinated by an N-terminal histidine. Following some initial confusion about the identity of the metal ion it has now been shown that these enzymes are copper-dependent oxygenases. Here we assess recent developments in the academic literature, focussing on the structures of the copper active sites. We provide critical comparisons with known small-molecules studies of copper-oxygen complexes and with copper methane monoxygenase, another of nature's powerful copper oxygenases.
authors.affiliation: Department of Chemistry, University of York, Heslington, York YO10 5DD, UK.
authors.forename: Glyn R
authors.initials: GR
authors.lastname: Hemsworth
authors.forename: Gideon J
authors.initials: GJ
authors.lastname: Davies
authors.forename: Paul H
authors.initials: PH
authors.lastname: Walton
mesh_terms: D001419:Bacteria / Q000201:enzymology; D020134:Catalytic Domain; D003300:Copper / Q000737:chemistry* / Q000378:metabolism; D005658:Fungi / Q000201:enzymology; D006639:Histidine / Q000378:metabolism; D008745:Methylation; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism; D010105:Oxygenases / Q000737:chemistry* / Q000378:metabolism; D011134:Polysaccharides / Q000378:metabolism
chemical_list: D011134:Polysaccharides; D006639:Histidine; D003300:Copper; D010105:Oxygenases; D010100:Oxygen