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Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Schittmayer, M; Birner-Gruenberger, R.
Lipolytic proteomics.
Mass Spectrom Rev. 2012; 31(5):570-582
Doi: 10.1002/mas.20355
Web of Science
PubMed
FullText
FullText_MUG
- Führende Autor*innen der Med Uni Graz
- Birner-Grünberger Ruth
- Schittmayer-Schantl Matthias
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- Abstract:
- Activity-based proteomics (ABP) employs small molecular probes to specifically label sets of enzymes based on their shared catalytic mechanism. Given that the vast majority of lipases belong to the family of serine hydrolases and share a nucleophilic active-site serine as part of a catalytic triad, activity-based probes are ideal tools to study lipases and lipolysis. Moreover, the ability of ABP to highlight or isolate specific subproteomes results in a massive decrease of sample complexity. Thereby, in-depth analysis of enzymes of interest with mass spectrometry becomes feasible. In this review, we cover probe design, technological developments, and applications of ABP of lipases, as well as give an overview of relevant identified proteins.
- Find related publications in this database (using NLM MeSH Indexing)
- Animals -
- Catalytic Domain -
- Humans -
- Lipase - analysis
- Lipolysis -
- Proteomics - methods
- Find related publications in this database (Keywords)
- activity-based proteomics
- lipid metabolism
- lipases