Dissemin is shutting down on January 1st, 2025

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Nature Research, Nature Chemical Biology, 11(7), p. 763-765, 2011

DOI: 10.1038/nchembio.659

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

Journal article published in 2011 by Jonathan Z. Long, Justin S. Cisar, David Milliken, Sherry Niessen, Chu Wang, Sunia A. Trauger, Gary Siuzdak ORCID, Benjamin F. Cravatt
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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 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 physiological relevance of our substrate assignments.