| First Author | Long JZ | Year | 2011 |
| Journal | Nat Chem Biol | Volume | 7 |
| Issue | 11 | Pages | 763-5 |
| PubMed ID | 21926997 | Mgi Jnum | J:218371 |
| Mgi Id | MGI:5617348 | Doi | 10.1038/nchembio.659 |
| Citation | Long JZ, et al. (2011) Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids. Nat Chem Biol 7(11):763-5 |
| abstractText | All organisms, including humans, possess a huge number of uncharacterized enzymes. Here we describe a general cell-based screen for enzyme substrate discovery by untargeted metabolomics and its application to identify the protein alpha/beta-hydrolase domain-containing 3 (ABHD3) as a lipase that selectively cleaves medium-chain and oxidatively truncated phospholipids. Abhd3(-/-) mice possess elevated myristoyl (C14)-phospholipids, including the bioactive lipid C14-lysophosphatidylcholine, confirming the physiological relevance of our substrate assignments. |
