5no7
From Proteopedia
Crystal Structure of a Xylan-active Lytic Polysaccharide Monooxygenase from Pycnoporus coccineus.
Structural highlights
FunctionLP14B_TRAC3 Lytic polysaccharide monooxygenase (LPMO) that oxidatively cleaves xylan with both C1 and C4 regioselectivity and that specifically targets the protective shield made by heteroxylans that cover cellulose microfibrils in wood (PubMed:29377002, PubMed:32793303). Catalysis by LPMOs requires the reduction of the active-site copper from Cu(II) to Cu(I) by a reducing agent and H(2)O(2) or O(2) as a cosubstrate (PubMed:29377002). Cleavage occurs only when xylans are bound to cellulose and not when they are in solution (PubMed:29377002). Increases the efficiency of wood saccharification through oxidative cleavage of highly refractory xylan-coated cellulose fibers via synergistic relationship with xylan-active enzymes, xylobiohydrolases and cellobiohydrolases (PubMed:29377002, PubMed:32793303).[1] [2] Publication Abstract from PubMedWood biomass is the most abundant feedstock envisioned for the development of modern biorefineries. However, the cost-effective conversion of this form of biomass into commodity products is limited by its resistance to enzymatic degradation. Here we describe a new family of fungal lytic polysaccharide monooxygenases (LPMOs) prevalent among white-rot and brown-rot basidiomycetes that is active on xylans-a recalcitrant polysaccharide abundant in wood biomass. Two AA14 LPMO members from the white-rot fungus Pycnoporus coccineus substantially increase the efficiency of wood saccharification through oxidative cleavage of highly refractory xylan-coated cellulose fibers. The discovery of this unique enzyme activity advances our knowledge on the degradation of woody biomass in nature and offers an innovative solution for improving enzyme cocktails for biorefinery applications. Lytic xylan oxidases from wood-decay fungi unlock biomass degradation.,Couturier M, Ladeveze S, Sulzenbacher G, Ciano L, Fanuel M, Moreau C, Villares A, Cathala B, Chaspoul F, Frandsen KE, Labourel A, Herpoel-Gimbert I, Grisel S, Haon M, Lenfant N, Rogniaux H, Ropartz D, Davies GJ, Rosso MN, Walton PH, Henrissat B, Berrin JG Nat Chem Biol. 2018 Jan 29. pii: nchembio.2558. doi: 10.1038/nchembio.2558. PMID:29377002[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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