Liquid Chromatography-Tandem Mass Spectrometry to Define Sortase Cleavage Products.
Bacterial Cell Wall Homeostasis
Methods in molecular biology, January 2016
Andrew Duong, Kalinka Koteva, Danielle L. Sexton, Marie A. Elliot
Sortase enzymes have specific endopeptidase activity, cleaving within a defined pentapeptide sequence at the C-terminal end of their protein substrates. Here, we describe how monitoring sortase cleavage activity can be achieved using peptide substrates. Peptide cleavage can be readily analyzed by liquid chromatography/tandem mass spectrometry (LC/MS/MS), which allows for the precise definition of cleavage sites. This technique could be used to analyze the peptidase activity of any enzyme, and identify sites of cleavage within any peptide.
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