A calcium-dependent acyltransferase that produces N-acyl phosphatidylethanolamines
An activity-based proteomic strategy identifies PLA2G4E as the calcium-dependent N-acyltransferase that generates an unusual triacylated class of lipids, the NAPEs, which are precursors to bioactive lipids including the endogenous cannabinoid anandamide. More than 30 years ago, a calcium-dependent e...
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| Veröffentlicht in: | Nature chemical biology 2016-09, Vol.12 (9), p.669-671 |
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| creator | Ogura, Yuji Parsons, William H Kamat, Siddhesh S Cravatt, Benjamin F |
| description | An activity-based proteomic strategy identifies PLA2G4E as the calcium-dependent N-acyltransferase that generates an unusual triacylated class of lipids, the NAPEs, which are precursors to bioactive lipids including the endogenous cannabinoid anandamide.
More than 30 years ago, a calcium-dependent enzyme activity was described that generates
N
-acyl phosphatidylethanolamines (NAPEs), which are precursors for
N
-acyl ethanolamine (NAE) lipid transmitters, including the endocannabinoid anandamide. The identity of this calcium-dependent N-acyltransferase (Ca-NAT) has remained mysterious. Here, we use activity-based protein profiling to identify the poorly characterized serine hydrolase PLA2G4E as a mouse brain Ca-NAT and show that this enzyme generates NAPEs and NAEs in mammalian cells. |
| doi_str_mv | 10.1038/nchembio.2127 |
| format | Article |
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More than 30 years ago, a calcium-dependent enzyme activity was described that generates
N
-acyl phosphatidylethanolamines (NAPEs), which are precursors for
N
-acyl ethanolamine (NAE) lipid transmitters, including the endocannabinoid anandamide. The identity of this calcium-dependent N-acyltransferase (Ca-NAT) has remained mysterious. Here, we use activity-based protein profiling to identify the poorly characterized serine hydrolase PLA2G4E as a mouse brain Ca-NAT and show that this enzyme generates NAPEs and NAEs in mammalian cells.</description><identifier>ISSN: 1552-4450</identifier><identifier>EISSN: 1552-4469</identifier><identifier>DOI: 10.1038/nchembio.2127</identifier><identifier>PMID: 27399000</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>631/45/287/1194 ; 631/92/607 ; 82 ; 82/58 ; 82/83 ; Acyltransferases - chemistry ; Acyltransferases - metabolism ; Animals ; Biochemical Engineering ; Biochemistry ; Bioorganic Chemistry ; brief-communication ; Calcium ; Calcium - metabolism ; Calcium phosphates ; Cell Biology ; Chemistry ; Chemistry/Food Science ; Enzymatic activity ; Enzymes ; Lipids ; Male ; Mammals ; Mice ; Mice, Inbred C57BL ; Molecular Structure ; Phosphatidylethanolamines - biosynthesis ; Phosphatidylethanolamines - chemistry</subject><ispartof>Nature chemical biology, 2016-09, Vol.12 (9), p.669-671</ispartof><rights>Springer Nature America, Inc. 2016</rights><rights>Copyright Nature Publishing Group Sep 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c487t-f6e31811e8cebc66930ff4799a1310f611f5b2e94390c2693e593a671c9159e83</citedby><cites>FETCH-LOGICAL-c487t-f6e31811e8cebc66930ff4799a1310f611f5b2e94390c2693e593a671c9159e83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27399000$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ogura, Yuji</creatorcontrib><creatorcontrib>Parsons, William H</creatorcontrib><creatorcontrib>Kamat, Siddhesh S</creatorcontrib><creatorcontrib>Cravatt, Benjamin F</creatorcontrib><title>A calcium-dependent acyltransferase that produces N-acyl phosphatidylethanolamines</title><title>Nature chemical biology</title><addtitle>Nat Chem Biol</addtitle><addtitle>Nat Chem Biol</addtitle><description>An activity-based proteomic strategy identifies PLA2G4E as the calcium-dependent N-acyltransferase that generates an unusual triacylated class of lipids, the NAPEs, which are precursors to bioactive lipids including the endogenous cannabinoid anandamide.
More than 30 years ago, a calcium-dependent enzyme activity was described that generates
N
-acyl phosphatidylethanolamines (NAPEs), which are precursors for
N
-acyl ethanolamine (NAE) lipid transmitters, including the endocannabinoid anandamide. The identity of this calcium-dependent N-acyltransferase (Ca-NAT) has remained mysterious. 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nature chemical biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ogura, Yuji</au><au>Parsons, William H</au><au>Kamat, Siddhesh S</au><au>Cravatt, Benjamin F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A calcium-dependent acyltransferase that produces N-acyl phosphatidylethanolamines</atitle><jtitle>Nature chemical biology</jtitle><stitle>Nat Chem Biol</stitle><addtitle>Nat Chem Biol</addtitle><date>2016-09-01</date><risdate>2016</risdate><volume>12</volume><issue>9</issue><spage>669</spage><epage>671</epage><pages>669-671</pages><issn>1552-4450</issn><eissn>1552-4469</eissn><abstract>An activity-based proteomic strategy identifies PLA2G4E as the calcium-dependent N-acyltransferase that generates an unusual triacylated class of lipids, the NAPEs, which are precursors to bioactive lipids including the endogenous cannabinoid anandamide.
More than 30 years ago, a calcium-dependent enzyme activity was described that generates
N
-acyl phosphatidylethanolamines (NAPEs), which are precursors for
N
-acyl ethanolamine (NAE) lipid transmitters, including the endocannabinoid anandamide. The identity of this calcium-dependent N-acyltransferase (Ca-NAT) has remained mysterious. Here, we use activity-based protein profiling to identify the poorly characterized serine hydrolase PLA2G4E as a mouse brain Ca-NAT and show that this enzyme generates NAPEs and NAEs in mammalian cells.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>27399000</pmid><doi>10.1038/nchembio.2127</doi><tpages>3</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1552-4450 |
| ispartof | Nature chemical biology, 2016-09, Vol.12 (9), p.669-671 |
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| subjects | 631/45/287/1194 631/92/607 82 82/58 82/83 Acyltransferases - chemistry Acyltransferases - metabolism Animals Biochemical Engineering Biochemistry Bioorganic Chemistry brief-communication Calcium Calcium - metabolism Calcium phosphates Cell Biology Chemistry Chemistry/Food Science Enzymatic activity Enzymes Lipids Male Mammals Mice Mice, Inbred C57BL Molecular Structure Phosphatidylethanolamines - biosynthesis Phosphatidylethanolamines - chemistry |
| title | A calcium-dependent acyltransferase that produces N-acyl phosphatidylethanolamines |
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