Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase

نویسندگان

  • Leila Lo Leggio
  • Thomas J. Simmons
  • Jens-Christian N. Poulsen
  • Kristian E. H. Frandsen
  • Glyn R. Hemsworth
  • Mary A. Stringer
  • Pernille von Freiesleben
  • Morten Tovborg
  • Katja S. Johansen
  • Leonardo De Maria
  • Paul V. Harris
  • Chee-Leong Soong
  • Paul Dupree
  • Theodora Tryfona
  • Nicolas Lenfant
  • Bernard Henrissat
  • Gideon J. Davies
  • Paul H. Walton
چکیده

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.

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عنوان ژورنال:

دوره 6  شماره 

صفحات  -

تاریخ انتشار 2015