| Structural highlights
Function
LP14B_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 PubMed
Wood 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 Also
References
- ↑ 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. Lytic xylan oxidases from wood-decay fungi unlock biomass degradation. Nat Chem Biol. 2018 Jan 29. pii: nchembio.2558. doi: 10.1038/nchembio.2558. PMID:29377002 doi:http://dx.doi.org/10.1038/nchembio.2558
- ↑ Zerva A, Pentari C, Grisel S, Berrin JG, Topakas E. A new synergistic relationship between xylan-active LPMO and xylobiohydrolase to tackle recalcitrant xylan. Biotechnol Biofuels. 2020 Aug 10;13:142. PMID:32793303 doi:10.1186/s13068-020-01777-x
- ↑ 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. Lytic xylan oxidases from wood-decay fungi unlock biomass degradation. Nat Chem Biol. 2018 Jan 29. pii: nchembio.2558. doi: 10.1038/nchembio.2558. PMID:29377002 doi:http://dx.doi.org/10.1038/nchembio.2558
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