Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase
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Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase. / Lo Leggio, Leila; Simmons, Thomas J.; Poulsen, Jens-Christian Navarro; Frandsen, Kristian Erik Høpfner; Hemsworth, Glyn R.; Stringer, Mary A.; von Freiesleben, Pernille; Tovborg, Morten; Johansen, Katja Salomon; De Maria, Leonardo; Harris, Paul V.; Soong, Chee-Leong; Dupree, Paul; Tryfona, Theodora; Lenfant, Nicolas; Henrissat, Bernard; Davies, Gideon J.; Walton, Paul H.
In: Nature Communications, Vol. 6, 5961, 2015.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase
AU - Lo Leggio, Leila
AU - Simmons, Thomas J.
AU - Poulsen, Jens-Christian Navarro
AU - Frandsen, Kristian Erik Høpfner
AU - Hemsworth, Glyn R.
AU - Stringer, Mary A.
AU - von Freiesleben, Pernille
AU - Tovborg, Morten
AU - Johansen, Katja Salomon
AU - De Maria, Leonardo
AU - Harris, Paul V.
AU - Soong, Chee-Leong
AU - Dupree, Paul
AU - Tryfona, Theodora
AU - Lenfant, Nicolas
AU - Henrissat, Bernard
AU - Davies, Gideon J.
AU - Walton, Paul H.
PY - 2015
Y1 - 2015
N2 - Lytic 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 β-amylase. The detailed structure of the enzyme's active site yields insights into the mechanism of action of this important class of enzymes.
AB - Lytic 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 β-amylase. The detailed structure of the enzyme's active site yields insights into the mechanism of action of this important class of enzymes.
U2 - 10.1038/ncomms6961
DO - 10.1038/ncomms6961
M3 - Journal article
C2 - 25608804
VL - 6
JO - Nature Communications
JF - Nature Communications
SN - 2041-1723
M1 - 5961
ER -
ID: 130691568