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Activity‐Based Probes for Studying the Activity of Flavin‐Dependent Oxidases and for the Protein Target Profiling of Monoamine Oxidase Inhibitors
Author(s) -
Krysiak Joanna M.,
Kreuzer Johannes,
Macheroux Peter,
Hermetter Albin,
Sieber Stephan A.,
Breinbauer Rolf
Publication year - 2012
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201201955
Subject(s) - flavin group , monoamine oxidase , monoamine oxidase b , flavin adenine dinucleotide , chemistry , flavoprotein , monoamine oxidase a , biochemistry , monoamine neurotransmitter , rasagiline , mechanism of action , enzyme , cofactor , parkinson's disease , disease , medicine , in vitro , serotonin , receptor , pathology
High profile : New activity‐based protein profiling (ABPP) probes have been designed that target exclusively monoamine oxidases A and B within living cells (see picture; FAD=flavin adenine dinucleotide, FMN=flavin monodinucleotide). With these probes it could be shown that the MAO inhibitor deprenyl, which is in clinical use against Parkinson's disease, shows unique protein specificity despite its covalent mechanism of action.