Structural and functional variation of chitin-binding domains of a lytic polysaccharide monooxygenase from Cellvibrio japonicus

(2012) NMR structure of a lytic polysaccharide monooxygenase provides insight into copper binding, protein dynamics, and substrate interactions.. (2009) The expression of

Conversion of  -chitin substrates with varying particle size and crystallinity reveals substrate preferences of the chitinases and lytic polysaccharide monooxygenase of

In ChiA, aromatic residues located on the chitin binding domain and on the glycon side (substrate binding subsites) of the active site are crucial for binding crystalline chitin

Here, we made a thorough characterization of HCHT in terms of the mode of action, processivity, binding, and rate constants for the cataly- sis and dissociation using α-chitin

Overall, the electronic changes to the copper SOMO in chitin- active AA10 LPMOs that occur upon addition of substrate are as follows: a reduction in the asymmetry of the

In order to easily monitor the chitin bind- ing activity of ChBD CHIT1 , we inserted the 49 C-terminal residues of HCHT into the BlaP β-lactamase and the chitin binding activity of

Kracher D, Andlar M, Furtmuller PG, Ludwig R: Active-site copper reduction promotes substrate binding of fungal lytic polysaccharide monooxygenase and reduces stability. Hangasky

Degradation of crystalline β-chitin with Chitobiase in combination with other chitin degrading enzymes from S.marcescens (ChiB, ChiC and CBP21) was observed to reveal