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

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 α/β-hydrolase domain-containing 3 (ABHD3) as a lipase that selectively cleaves me...

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Autores principales: Long, Jonathan Z., Cisar, Justin S., Milliken, David, Niessen, Sherry, Wang, Chu, Trauger, Sunia A., Siuzdak, Gary, Cravatt, Benjamin F.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2011
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3201731/
https://www.ncbi.nlm.nih.gov/pubmed/21926997
http://dx.doi.org/10.1038/nchembio.659
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author Long, Jonathan Z.
Cisar, Justin S.
Milliken, David
Niessen, Sherry
Wang, Chu
Trauger, Sunia A.
Siuzdak, Gary
Cravatt, Benjamin F.
author_facet Long, Jonathan Z.
Cisar, Justin S.
Milliken, David
Niessen, Sherry
Wang, Chu
Trauger, Sunia A.
Siuzdak, Gary
Cravatt, Benjamin F.
author_sort Long, Jonathan Z.
collection PubMed
description 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 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.
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spelling pubmed-32017312012-05-01 Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids Long, Jonathan Z. Cisar, Justin S. Milliken, David Niessen, Sherry Wang, Chu Trauger, Sunia A. Siuzdak, Gary Cravatt, Benjamin F. Nat Chem Biol Article 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 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. 2011-09-18 /pmc/articles/PMC3201731/ /pubmed/21926997 http://dx.doi.org/10.1038/nchembio.659 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Long, Jonathan Z.
Cisar, Justin S.
Milliken, David
Niessen, Sherry
Wang, Chu
Trauger, Sunia A.
Siuzdak, Gary
Cravatt, Benjamin F.
Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids
title Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids
title_full Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids
title_fullStr Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids
title_full_unstemmed Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids
title_short Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids
title_sort metabolomics annotates abhd3 as a physiologic regulator of medium-chain phospholipids
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3201731/
https://www.ncbi.nlm.nih.gov/pubmed/21926997
http://dx.doi.org/10.1038/nchembio.659
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