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

Academic Article
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Overview

related to degree

  • Long, Jonathan, Ph.D. in Chemistry, Scripps Research 2007 - 2011

authors

  • Long, Jonathan
  • Cisar, J. S.
  • Milliken, D.
  • Niessen, Sherry
  • Wang, C.
  • Trauger, S. A.
  • Siuzdak, Gary
  • Cravatt, Benjamin

publication date

  • November 2011

journal

  • Nature Chemical Biology  Journal

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.

subject areas

  • Animals
  • Gene Expression Regulation
  • Gene Expression Regulation, Enzymologic
  • HEK293 Cells
  • Humans
  • Hydrolases
  • Membrane Proteins
  • Metabolomics
  • Mice
  • Mice, Knockout
  • Phospholipids
  • Small Molecule Libraries
  • Substrate Specificity
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Identity

PubMed Central ID

  • PMC3201731

International Standard Serial Number (ISSN)

  • 1552-4450

Digital Object Identifier (DOI)

  • 10.1038/nchembio.659

PubMed ID

  • 21926997
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Additional Document Info

start page

  • 763

end page

  • 765

volume

  • 7

issue

  • 11

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