| Structural highlights
Function
Q8A3I4_BACTN
Publication Abstract from PubMed
GH29 alpha-l-fucosidases catalyze the hydrolysis of alpha-l-fucosidic linkages. Deficiency in human lysosomal alpha-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 alpha-l-fucosidases from bacteria, mice and man. Crystallographic analysis on bacterial alpha-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 alpha-l-fucosidase inhibitor from eight configurational isomers.
In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 alpha-l-fucosidases.,Jiang J, Kallemeijn WW, Wright DW, van den Nieuwendijk AMCH, Rohde VC, Folch EC, van den Elst H, Florea BI, Scheij S, Donker-Koopman WE, Verhoek M, Li N, Schurmann M, Mink D, Boot RG, Codee JDC, van der Marel GA, Davies GJ, Aerts JMFG, Overkleeft HS Chem Sci. 2015 May 1;6(5):2782-false. doi: 10.1039/c4sc03739a. Epub 2015 Feb 9. PMID:29142681[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Jiang J, Kallemeijn WW, Wright DW, van den Nieuwendijk AMCH, Rohde VC, Folch EC, van den Elst H, Florea BI, Scheij S, Donker-Koopman WE, Verhoek M, Li N, Schurmann M, Mink D, Boot RG, Codee JDC, van der Marel GA, Davies GJ, Aerts JMFG, Overkleeft HS. In vitro and in vivo comparative and competitive activity-based protein profiling of GH29 alpha-l-fucosidases. Chem Sci. 2015 May 1;6(5):2782-false. doi: 10.1039/c4sc03739a. Epub 2015 Feb 9. PMID:29142681 doi:http://dx.doi.org/10.1039/c4sc03739a
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