Related Experiment Video
Updated: Mar 27, 2026

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
Published on: October 3, 2018
Structural and functional characterization of a small chitin-active lytic polysaccharide monooxygenase domain of a
Sophanit Mekasha1, Zarah Forsberg1, Bjørn Dalhus2,3
1Department of Chemistry, Biotechnology and Food Science, Norwegian University of Life Sciences, Ås, Norway.
Abstract:
Lytic polysaccharide monooxygenases (LPMOs) boost enzymatic depolymerization of recalcitrant polysaccharides, such as chitin and cellulose. We have studied a chitin-active LPMO domain (JdLPMO10A) that is considerably smaller (15.5 kDa) than all structurally characterized LPMOs so far and that is part of a modular protein containing a GH18 chitinase. The 1.55 Å resolution structure revealed deletions of interacting loops that protrude from the core β-sandwich scaffold in larger LPMO10s. Despite these deletions, the enzyme is active on alpha- and beta-chitin, and the chitin-binding surface previously described for larger LPMOs is fully conserved. JdLPMO10A may represent a minimal scaffold needed to catalyse the powerful LPMO reaction.
Related Concept Videos
Inorganic Nitrogen Assimilation
Microbes and Methanogenesis
Anoxygenic Phototrophic Bacteria
Prokaryotic Gene Structure and Organization
Metabolism of Chemolithotrophs
Structure of Porins

