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

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.

journal_name

Bioorg Med Chem

authors

Nickel S,Kaschani F,Colby T,van der Hoorn RA,Kaiser M

doi

10.1016/j.bmc.2011.06.041

subject

Has Abstract

pub_date

2012-01-15 00:00:00

pages

601-6

issue

2

eissn

0968-0896

issn

1464-3391

pii

S0968-0896(11)00481-0

journal_volume

20

pub_type

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