Abstract
Activity-based proteomic profiling (ABPP) enables the functional study of enzymes by employing small molecule probes that bind covalently to the active site of an enzyme. Activity-based probes can penetrate cells and tissues and thereby allow enzymes to be targeted/labelled in their native state. Probes can be designed to target individual enzymes or whole enzyme groups, which makes ABPP a versatile protein profiling technique. In this review, we give an overview of research advances through ABPP in the context of lipid hydrolase research. We report of lipid hydrolases that were discovered and characterized through ABPP, and aim to give an overview of commonly used probes as well as inhibitors that were discovered and characterized by competitive ABPP. Lastly, this review aims to raise caveats and current limitations of this protein profiling technique.
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Honeder, S. E., Tomin, T., Schinagl, M., Pfleger, R., Hoehlschen, J., Darnhofer, B., … Birner-Gruenberger, R. (2023, March 1). Research Advances Through Activity-Based Lipid Hydrolase Profiling. Israel Journal of Chemistry. John Wiley and Sons Inc. https://doi.org/10.1002/ijch.202200078
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