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Issue 5, 2015
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In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 α-L-fucosidases

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Abstract

GH29 α-L-fucosidases catalyze the hydrolysis of α-L-fucosidic linkages. Deficiency in human lysosomal α-L-fucosidase (FUCA1) leads to the recessively inherited disorder, fucosidosis. Herein we describe the development of fucopyranose-configured cyclophellitol aziridines as activity-based probes (ABPs) for selective in vitro and in vivo labeling of GH29 α-L-fucosidases from bacteria, mice and man. Crystallographic analysis on bacterial α-L-fucosidase confirms that the ABPs act by covalent modification of the active site nucleophile. Competitive activity-based protein profiling identified L-fuconojirimycin as the single GH29 α-L-fucosidase inhibitor from eight configurational isomers.

Graphical abstract: In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 α-l-fucosidases

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Publication details

The article was received on 03 Dec 2014, accepted on 09 Feb 2015 and first published on 09 Feb 2015


Article type: Edge Article
DOI: 10.1039/C4SC03739A
Citation: Chem. Sci., 2015,6, 2782-2789
  • Open access: Creative Commons BY license
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    In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 α-L-fucosidases

    J. Jiang, W. W. Kallemeijn, D. W. Wright, A. M. C. H. van den Nieuwendijk, V. C. Rohde, E. C. Folch, H. van den Elst, B. I. Florea, S. Scheij, W. E. Donker-Koopman, M. Verhoek, N. Li, M. Schürmann, D. Mink, R. G. Boot, J. D. C. Codée, G. A. van der Marel, G. J. Davies, J. M. F. G. Aerts and H. S. Overkleeft, Chem. Sci., 2015, 6, 2782
    DOI: 10.1039/C4SC03739A

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