| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1375879 | Bioorganic & Medicinal Chemistry Letters | 2009 | 4 Pages |
Aryl sulfamates were originally developed as inhibitors of steroid sulfatase, and have recently been shown to be powerful inactivators of a bacterial sulfatase, PaAtsA from Pseudomonas aeruginosa. We demonstrate that a simple aryl sulfamate, 3-nitrophenyl sulfamate, can inactivate sulfatases from various sources including snail, limpet and abalone. In each case inactivation was time-dependent and active-site directed, as demonstrated by protection against inactivation by substrate. These results suggest that such easily acquired aryl sulfamates can be used as reliable biochemical reagents for the study of sulfatases from a diverse array of sources.
Graphical abstractAryl sulfamates were identified as versatile active-site directed inactivators for a range of sulfatases. They are promising tools for analysis of sulfatase-related processes and for the treatment of associated dysfunctions in vivo.Figure optionsDownload full-size imageDownload as PowerPoint slide
