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Bioorg Med Chem. 2012 Jan 15;20(2):601-6. doi: 10.1016/j.bmc.2011.06.041. Epub 2011 Jul 15.

A para-nitrophenol phosphonate probe labels distinct serine hydrolases of Arabidopsis.

Author information

1
Zentrum für Medizinische Biotechnologie, Fakultät Biologie, Universität Duisburg-Essen, Universitätsstr. 2, D-45117 Essen, Germany.

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.

PMID:
21763150
DOI:
10.1016/j.bmc.2011.06.041
[Indexed for MEDLINE]

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