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A para-nitrophenol phosphonate probe labels distinct serine hydrolases of Arabidopsis |
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| Authors: | Sabrina Nickel Farnusch Kaschani Tom Colby Renier A.L. van der Hoorn Markus Kaiser |
| Affiliation: | 1. Zentrum für Medizinische Biotechnologie, Fakultät Biologie, Universität Duisburg-Essen, Universitätsstr. 2, D-45117 Essen, Germany;2. The Plant Chemetics Laboratory, Chemical Genomics Centre of the Max Planck Society, Max Planck Institute for Plant Breeding Research, Carl-von-Linne-Weg 10, D-50829 Cologne, Germany;3. Mass Spectrometry Group, Max Planck Institute for Plant Breeding Research, Carl-von-Linne-Weg 10, D-50829 Cologne, Germany;1. Universiteit Leiden, Leiden Inst. of Chemistry, Postbus 9502, Leiden, 2300 RA, Netherlands |
| Abstract: | Activity-based protein profiling represents a powerful methodology to probe the activity state of enzymes under various physiological conditions. Here we present the development of a para-nitrophenol phosphonate activity-based probe with structural similarities to the potent agrochemical paraoxon. We demonstrate that this probes labels distinct serine hydrolases with the carboxylesterase CXE12 as the predominant target in Arabidopsis thaliana. The designed probe features a distinct labeling pattern and therefore represents a promising chemical tool to investigate physiological roles of selected serine hydrolases such as CXE12 in plant biology. |
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