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Nat Commun. 2015 Jan 22;6:5961. doi: 10.1038/ncomms6961.

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

Author information

1
Department of Chemistry, University of Copenhagen, Universitetsparken 5, 2100 Copenhagen Ø, Denmark.
2
Department of Biochemistry, University Of Cambridge, Tennis Court Road, Cambridge CB2 1QW, UK.
3
Department of Chemistry, University of York, York YO10 5DD, UK.
4
Novozymes A/S, Krogshoejvej 36, 2880 Bagsvaerd, Denmark.
5
Novozymes, Inc., 1445 Drew Avenue, Davis, California 95618, USA.
6
Novozymes North America Inc., 77 Perrys Chapel Church Road, Franklinton, North Carolina 27525, USA.
7
Architecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, 13288 Marseille, France.
8
1] Architecture et Fonction des Macromolécules Biologiques, CNRS, Aix-Marseille Université, 13288 Marseille, France [2] Department of Biological Sciences, King Abdulaziz University, Jeddah, Saudi Arabia.

Abstract

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.

PMID:
25608804
PMCID:
PMC4338556
DOI:
10.1038/ncomms6961
[Indexed for MEDLINE]
Free PMC Article

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