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Activity, stability and 3-D structure of the Cu( ii ) form of a chitin-active lytic polysaccharide monooxygenase from Bacillus amyloliquefaciens

DOI: 10.1039/C6DT02793H DOI Help

Authors: Rebecca C. Gregory (Structural Biology Laboratory, University of York) , Glyn R. Hemsworth (Structural Biology Laboratory, University of York) , Johan P. Turkenburg (Structural Biology Laboratory, University of York) , Samuel J. Hart (Structural Biology Laboratory, University of York) , Paul H. Walton (Department of Chemistry, University of York) , Gideon J. Davies (Structural Biology Laboratory, University of York)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Dalton Trans. , VOL 45 , PAGES 16904 - 16912

State: Published (Approved)
Published: September 2016
Diamond Proposal Number(s): 9948

Abstract: The enzymatic deconstruction of recalcitrant polysaccharide biomass is central to the conversion of these substrates for societal benefit, such as in biofuels. Traditional models for enzyme-catalysed polysaccharide degradation involved the synergistic action of endo-, exo- and processive glycoside hydrolases working in concert to hydrolyse the substrate. More recently this model has been succeeded by one featuring a newly discovered class of mononuclear copper enzymes: lytic polysaccharide monooxygenases (LPMOs; classified as Auxiliary Activity (AA) enzymes in the CAZy classification). In 2013, the structure of an LPMO from Bacillus amyloliquefaciens, BaAA10, was solved with the Cu centre photoreduced to Cu(I) in the X-ray beam. Here we present the catalytic activity of BaAA10. We show that it is a chitin-active LPMO, active on both α and β chitin, with the Cu(II) binding with low nM KD, and the substrate greatly increasing the thermal stability of the enzyme. A spiral data collection strategy has been used to facilitate access to the previously unobservable Cu(II) state of the active centre, revealing a coordination geometry around the copper which is distorted from axial symmetry, consistent with the previous findings from EPR spectroscopy.

Subject Areas: Chemistry, Biology and Bio-materials

Instruments: I04-Macromolecular Crystallography

Added On: 14/11/2016 11:39

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