182227-44-7Relevant articles and documents
A versatile mechanism based reaction probe for the direct selection of biocatalysts
Lo, Lee-Chiang,Lo, Chih-Hung L.,Janda, Kim D.,Kassel, Daniel B.,Raushel, Frank M.
, p. 2117 - 2120 (1996)
A mechanism based reaction probe was synthesized and shown to modify a bacterial phosphotriesterase; this strategy for generating a probe is general and should allow the isolation of a host of unique catalysts.
Evaluation of sulfatase-directed quinone methide traps for proteomics
Lenger, Janina,Schr?der, Marius,Ennemann, Eva C.,Müller, Benjamin,Wong, Chi-Huey,Noll, Thomas,Dierks, Thomas,Hanson, Sarah R.,Sewald, Norbert
supporting information; scheme or table, p. 622 - 627 (2012/03/11)
Sulfatases hydrolytically cleave sulfate esters through a unique catalytic aldehyde, which is introduced by a posttranslational oxidation. To profile active sulfatases in health and disease, activity-based proteomic tools are needed. Herein, quinone methi
Activity-based fluorescent probes that target phosphatases
Zhu, Qing,Huang, Xuan,Chen, Grace Y. J.,Yao, Shao Q.
, p. 2669 - 2672 (2007/10/03)
We have successfully designed and synthesized two fluorescently-labeled, activity-based probes, Probe 1 and Probe 2, which were shown to label protein tyrosine phosphatases specifically, as well as other types of phosphatases. The probes were not reactive towards the other non-phosphatase enzymes tested. These probes may find potential applications in large-scale proteomic experiments whereby subclasses of proteins may be selectively identified.