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.
Original language | English (US) |
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Pages (from-to) | 34-42 |
Number of pages | 9 |
Journal | FEBS Letters |
Volume | 590 |
Issue number | 1 |
DOIs | |
State | Published - Jan 1 2016 |
Bibliographical note
Publisher Copyright:© 2015 Federation of European Biochemical Societies.
Keywords
- AA10
- Jonesia denitrificans
- chitin
- chitinase
- lytic polysaccharide monooxygenase