The role of Asp116 in the reductive cleavage of dioxygen to water in CotA laccase: assistance during the proton-transfer mechanism

The role of Asp116 in the pronotation events taking place during CotA laccase catalytic mechanism was investigated. The crystal structure determination of three distinct mutants (D116A, D116N and D116E), produced by site-saturation mutagenesis, together with theoretical calculations have provided evidence of its importance during the reductive cleavage of dioxygen to water.

Endo-β-D-1,4-mannanase from Chrysonilia sitophila displays a novel loop arrangement for substrate selectivity

The crystal structure of endo-β-D-1,4-mannanase from Chrysonilia sitophila has been solved at 1.40 Å. The enzyme has mixed activity as both an endo-mannanase and endo-glucanase and the crystal structure revealed a unique arrangement of three surface loops surrounding the active site, altering the topography of the binding cleft.