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Enzymology
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- EnzymologyOpen Access
High-resolution structure of a lytic polysaccharide monooxygenase from Hypocrea jecorina reveals a predicted linker as an integral part of the catalytic domain
Journal of Biological ChemistryVol. 292Issue 46p19099–19109Published online: September 12, 2017- Henrik Hansson
- Saeid Karkehabadi
- Nils Mikkelsen
- Nicholai R. Douglas
- Steve Kim
- Anna Lam
- and others
Cited in Scopus: 44For decades, the enzymes of the fungus Hypocrea jecorina have served as a model system for the breakdown of cellulose. Three-dimensional structures for almost all H. jecorina cellulose-degrading enzymes are available, except for HjLPMO9A, belonging to the AA9 family of lytic polysaccharide monooxygenases (LPMOs). These enzymes enhance the hydrolytic activity of cellulases and are essential for cost-efficient conversion of lignocellulosic biomass. Here, using structural and spectroscopic analyses, we found that native HjLPMO9A contains a catalytic domain and a family-1 carbohydrate-binding module (CBM1) connected via a linker sequence.