Samenvatting
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 bio-orthogonal 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.
Originele taal-2 | English |
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Pagina's (van-tot) | 399-408 |
Aantal pagina's | 10 |
Tijdschrift | MedChemCommun |
Volume | 7 |
Nummer van het tijdschrift | 3 |
DOI's | |
Status | Published - 2016 |