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I03-Macromolecular Crystallography	Glycosylated cyclophellitol-derived activity-based probes and inhibitors for cellulases Casper De Boer , Nicholas G. S. Mcgregor , Evert Peterse , Sybrin P. Schröder , Bogdan I. Florea , Jianbing Jiang , Jos Reijngoud , Arthur F. J. Ram , Gilles P. Van Wezel , Gijsbert A. Van Der Marel , Jeroen D. C. Codée , Herman S. Overkleeft , Gideon Davies Rsc Chemical Biology 25 DOI: 10.1039/D0CB00045K Diamond Proposal Number(s): [18598] Open Access Show Abstract ▼ Abstract: Cellulases and related β-1,4-glucanases are essential components of lignocellulose-degrading enzyme mixtures. The detection of β-1,4-glucanase activity typically relies on monitoring the breakdown of purified lignocellulose-derived substrates or synthetic chromogenic substrates, limiting the activities which can be detected and complicating the tracing of activity back to specific components within complex enzyme mixtures. As a tool for the rapid detection and identification of β-1,4-glucanases, a series of glycosylated cyclophellitol inhibitors mimicking β-1,4-glucan oligosaccharides have been synthesised. These compounds are highly efficient inhibitors of HiCel7B, a well-known GH7 endo-β-1,4-glucanase. An elaborated activity-based probe facilitated the direct detection and identification of β-1,4-glucanases within a complex fungal secretome without any detectable cross-reactivity with β-D-glucosidases. These probes and inhibitors add valuable new capacity to the growing toolbox of cyclophellitol-derived probes for the activity-based profiling of biomass-degrading enzymes.	Jul 2020

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I03-Macromolecular Crystallography

Glycosylated cyclophellitol-derived activity-based probes and inhibitors for cellulases