{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jiang J"],"funding":["European Research Council","Biotechnology and Biological Sciences Research Council"],"pagination":["2782-false"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5654414"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["6(5)"],"pubmed_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 <i>in vitro</i> and <i>in vivo</i> 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."],"journal":["Chemical science"],"pubmed_title":["&lt;i&gt;In vitro&lt;/i&gt; and &lt;i&gt;in vivo&lt;/i&gt; comparative and competitive activity-based protein profiling of GH29 α-l-fucosidases."],"pmcid":["PMC5654414"],"funding_grant_id":["322942","1094267"],"pubmed_authors":["van den Nieuwendijk AMCH","Jiang J","Donker-Koopman WE","Folch EC","Scheij S","Schurmann M","Verhoek M","Wright DW","van den Elst H","Davies GJ","Kallemeijn WW","Florea BI","Li N","van der Marel GA","Codee JDC","Overkleeft HS","Boot RG","Aerts JMFG","Rohde VC","Mink D"],"additional_accession":[]},"is_claimable":false,"name":"&lt;i&gt;In vitro&lt;/i&gt; and &lt;i&gt;in vivo&lt;/i&gt; comparative and competitive activity-based protein profiling of GH29 α-l-fucosidases.","description":"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 <i>in vitro</i> and <i>in vivo</i> 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.","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 May","modification":"2026-04-30T09:19:19.083Z","creation":"2019-03-26T23:02:45Z"},"accession":"S-EPMC5654414","cross_references":{"pubmed":["29142681"],"doi":["10.1039/c4sc03739a"]}}