LC-MS based metabolomics identifies a novel regulator of phospholipids

 

ABHD3 - a lipase of C14-phospholipids

All organisms possess a huge number of uncharacterized enzymes and metabolites. Long et al., performed a cell-based screen for enzyme substrate discovery by untargeted metabolomics using LC-MS. The group found the enzyme α/β-hydrolase domain-containing 3 (ABHD3) as a lipase that selectively cleaves C14-phospholipids.  The metabolites were identified by tandem MS fragmentation and co-elution with synthetic standards.

Further experiments showed that Abhd3(-/-) mice possess elevated myristoyl (C14)-phospholipids, including the bioactive lipid C14-lysophosphatidylcholine, confirming the physiological relevance of our substrate assignments.

These data nicely demonstrate the potential and options of mass spec based metabolomics.

 

 

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Long JZ, Cisar JS, Milliken D, Niessen S, Wang C, Trauger SA, Siuzdak G, Cravatt BF (2011), "Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids". Nature Chemical Biology 7(11): 763-65



Josef Ecker

6th December 2011