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


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 ?/?-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.

SUBMITTER: Long JZ 

PROVIDER: S-EPMC3201731 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature

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

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]

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