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From the same journal

Potent and selective activity-based probes for GH27 human retaining α-galactosidases

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Published copy (DOI)


  • Lianne I. Willems
  • Thomas J. M. Beenakker
  • Benjamin S. Murray
  • Saskia Scheij
  • Wouter W. Kallemeijn
  • Rolf G. Boot
  • Marri Verhoek
  • Wilma E. Donker-Koopman
  • Maria J. Ferraz
  • Erwin R. van Rijssel
  • Bogdan I. Florea
  • Jeroen D C Codée
  • Gijsbert A. Van Der Marel
  • Johannes M F G Aerts
  • Herman S. Overkleeft


Publication details

JournalJournal of the American Chemical Society
DateE-pub ahead of print - 8 Aug 2014
Issue number33
Number of pages4
Pages (from-to)11622-11625
Original languageEnglish


Lysosomal degradation of glycosphingolipids is mediated by the consecutive action of several glycosidases. Malfunctioning of one of these hydrolases can lead to a lysosomal storage disorder such as Fabry disease, which is caused by a deficiency in α-galactosidase A. Herein we describe the development of potent and selective activity-based probes that target retaining α-galactosidases. The fluorescently labeled aziridine-based probes 3 and 4 inhibit the two human retaining α-galactosidases αGal A and αGal B covalently and with high affinity. Moreover, they enable the visualization of the endogenous activity of both α-galactosidases in cell extracts, thereby providing a means to study the presence and location of active enzyme levels in different cell types, such as healthy cells versus those derived from Fabry patients.

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