Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids

Citation:

Long JZ, Cisar JS, Milliken D, Niessen S, Wang C, Trauger SA, Siuzdak G, Cravatt BF. Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids. Nat Chem Biol. 2011;7 :763-5.

Date Published:

Nov

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.

Notes:

Long, Jonathan ZCisar, Justin SMilliken, DavidNiessen, SherryWang, ChuTrauger, Sunia ASiuzdak, GaryCravatt, Benjamin FCA132630/CA/NCI NIH HHS/R01 CA132630-04/CA/NCI NIH HHS/Nat Chem Biol. 2011 Sep 18;7(11):763-5. doi: 10.1038/nchembio.659.

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