Bioorthogonal metabolic labelling with acyl-CoA reporters: targeting protein acylation†
Abstract
Protein acylation is an abundant post-translational modification with a pivotal role in a plethora of biological processes. To date, metabolic labelling with functionalized precursors of acyl-CoA and subsequent bioorthogonal ligation to a complementary detection tag has offered an attractive approach for monitoring endogenous protein acylation with excellent selectivity. This review focuses on the applications of alkyne- and alkene-based bioorthogonal chemistries in the study of enzyme activity in vitro and summarizes the carboxylate-type chemical reporters that have enabled the visualization and identification of cellular acylated proteins. However, despite their importance, serious limitations question the use of this two-step labelling method in the quantification of the protein acylome.