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 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.
Original language | English |
---|---|
Pages (from-to) | 399-408 |
Number of pages | 10 |
Journal | MedChemCommun |
Volume | 7 |
Issue number | 3 |
DOIs | |
Publication status | Published - 2016 |
Keywords
- CYTOSOLIC ACETYL-COENZYME
- OXIDATIVE HECK REACTION
- 1,3-DIPOLAR CYCLOADDITION REACTION
- ATP-CITRATE LYASE
- CHEMICAL REPORTERS
- CLICK CHEMISTRY
- FATTY-ACIDS
- POSTTRANSLATIONAL MODIFICATIONS
- TERMINAL ALKYNES
- HISTONE ACETYLTRANSFERASES