| Title : Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids - Long_2011_Nat.Chem.Biol_7_763 |
| Author(s) : Long JZ , Cisar JS , Milliken D , Niessen S , Wang C , Trauger SA , Siuzdak G , Cravatt BF |
| Ref : Nat Chemical Biology , 7 :763 , 2011 |
|
Abstract :
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. |
| PubMedSearch : Long_2011_Nat.Chem.Biol_7_763 |
| PubMedID: 21926997 |
| Gene_locus related to this paper: human-ABHD3 , mouse-abhd3 |
| Substrate | 1-Myristoyl-2-linoleoylphosphatidylcholine C14-lysophosphatidylcholine Dilauroyl-lecithin |
| Gene_locus | human-ABHD3 mouse-abhd3 |
| Family | abh_upf0017 |
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
Nat Chemical Biology
7 :763
Long JZ, Cisar JS, Milliken D, Niessen S, Wang C, Trauger SA, Siuzdak G, Cravatt BF (2011)
Nat Chemical Biology
7 :763