title: Fungal cellulose degradation by oxidative enzymes: from dysfunctional GH61 family to powerful lytic polysaccharide monooxygenase family.
abstract: Our understanding of fungal cellulose degradation has shifted dramatically in the past few years with the characterization of a new class of secreted enzymes, the lytic polysaccharide monooxygenases (LPMO). After a period of intense research covering structural, biochemical, theoretical and evolutionary aspects, we have a picture of them as wedge-like copper-dependent metalloenzymes that on reduction generate a radical copper-oxyl species, which cleaves mainly crystalline cellulose. The main biological function lies in the synergism of fungal LPMOs with canonical hydrolytic cellulases in achieving efficient cellulose degradation. Their important role in cellulose degradation is highlighted by the wide distribution and often numerous occurrences in the genomes of almost all plant cell-wall degrading fungi. In this review, we provide an overview of the latest achievements in LPMO research and consider the open questions and challenges that undoubtedly will continue to stimulate interest in this new and exciting group of enzymes.
authors.forename: Ingo
authors.initials: I
authors.lastname: Morgenstern
authors.forename: Justin
authors.initials: J
authors.lastname: Powlowski
authors.forename: Adrian
authors.initials: A
authors.lastname: Tsang
mesh_terms: D001203:Ascomycota / Q000201:enzymology*; D002482:Cellulose / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D006899:Mixed Function Oxygenases / Q000378:metabolism*; D011134:Polysaccharides / Q000378:metabolism*
chemical_list: D011134:Polysaccharides; D002482:Cellulose; D006899:Mixed Function Oxygenases; D006026:Glycoside Hydrolases
keywords: AA9; GH61; cellobiose dehydrogenase; oxidative cellulose degradation