Structural highlights
FunctionAA13_ASPOR Lytic polysaccharide monooxygenase-related protein that has no activity towards starch (PubMed:25608804). 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 (Probable).[1] Publication Abstract from PubMedLytic polysaccharide monooxygenases (LPMOs) are recently discovered enzymes that oxidatively deconstruct polysaccharides. LPMOs are fundamental in the effective utilization of these substrates by bacteria and fungi; moreover, the enzymes have significant industrial importance. We report here the activity, spectroscopy and three-dimensional structure of a starch-active LPMO, a representative of the new CAZy AA13 family. We demonstrate that these enzymes generate aldonic acid-terminated malto-oligosaccharides from retrograded starch and boost significantly the conversion of this recalcitrant substrate to maltose by beta-amylase. The detailed structure of the enzyme's active site yields insights into the mechanism of action of this important class of enzymes. Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase.,Lo Leggio L, Simmons TJ, Poulsen JC, Frandsen KE, Hemsworth GR, Stringer MA, von Freiesleben P, Tovborg M, Johansen KS, De Maria L, Harris PV, Soong CL, Dupree P, Tryfona T, Lenfant N, Henrissat B, Davies GJ, Walton PH Nat Commun. 2015 Jan 22;6:5961. doi: 10.1038/ncomms6961. PMID:25608804[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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