Sandgren, Mats
- Department of Molecular Sciences, Swedish University of Agricultural Sciences
Abstract
Lytic polysaccharide monooxygenases (LPMOs) are key enzymes for the biotechnological exploitation of lignocellulosic biomass, yet their efficient application depends on the in-depth understanding of their mechanism of action. Here, we describe the structural and mutational characterization of a C4-active LPMO from Myceliophthora thermophila, MtLPMO9F, that belongs to auxiliary activity family 9 (AA9). MtLPMO9F is active on cellulose, cello-oligosaccharides and xyloglucan. The crystal structure of MtLPMO9F catalytic domain, determined at 2.3 & Aring; resolution, revealed a double conformation for loop L3 with a potential implication in the formation of aglycon subsites. Product analysis of reactions with cello-oligosaccharides showed a prevalent -4 to +2 binding mode. Subsequent biochemical characterization of 4 MtLPMO9F point mutants further provided insights in LPMO structure-function relationships regarding both substrate binding and the role of second-coordination sphere residues.
Keywords
Lytic polysaccharide monooxygenase; Mutational study; Substrate specificity
Published in
International Journal of Biological Macromolecules
2025, volume: 288, article number: 138574
Publisher: ELSEVIER
SLU Authors
UKÄ Subject classification
Biochemistry
Molecular Biology
Publication identifier
- DOI: https://doi.org/10.1016/j.ijbiomac.2024.138574
Permanent link to this page (URI)
https://res.slu.se/id/publ/140175