Ontology highlight
ABSTRACT:
SUBMITTER: Long JZ
PROVIDER: S-EPMC3201731 | biostudies-literature | 2011 Sep
REPOSITORIES: biostudies-literature
Long Jonathan Z JZ Cisar Justin S JS Milliken David D Niessen Sherry S Wang Chu C Trauger Sunia A SA Siuzdak Gary G Cravatt Benjamin F BF
Nature chemical biology 20110918 11
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 α/β-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 ...[more]