Structural determinants of bacterial lytic polysaccharide monooxygenase functionality.

@article{Forsberg2018StructuralDO,
  title={Structural determinants of bacterial lytic polysaccharide monooxygenase functionality.},
  author={Zarah Forsberg and Bastien Bissaro and Jonathan Gullesen and Bj\orn Dalhus and Gustav Vaaje-Kolstad and Vincent G H Eijsink},
  journal={The Journal of biological chemistry},
  year={2018},
  volume={293 4},
  pages={1397-1412}
}
Bacterial lytic polysaccharide monooxygenases (LPMO10s) use redox chemistry to cleave glycosidic bonds in the two foremost recalcitrant polysaccharides found in nature, namely cellulose and chitin. Analysis of correlated mutations revealed that the substrate-binding and copper-containing surface of LPMO10s composes a network of co-evolved residues and interactions, whose roles in LPMO functionality are unclear. Here, we mutated a subset of these correlated residues in a newly characterized C1… CONTINUE READING