Download MendeleyGlycosylated cyclophellitol-derived activity-based probes and inhibitors for cellulases.
de Boer, C., McGregor, N.G.S., Peterse, E., Schroder, S.P., Florea, B.I., Jiang, J., Reijngoud, J., Ram, A.F.J., van Wezel, G.P., van der Marel, G.A., Codee, J.D.C., Overkleeft, H.S., Davies, G.J.(2020) RSC Chem Biol 1: 148-155
- PubMed: 34458755
- DOI: https://doi.org/10.1039/d0cb00045k
- Primary Citation of Related Structures:
6YOZ, 6YP1 - PubMed 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.
Organizational Affiliation:
Leiden Institute of Chemistry, Leiden University Einsteinweg 55 2300 RA Leiden The Netherlands [email protected].
