Enzymes
| UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
- Name help_outline 1-hexadecanoyl-sn-glycero-3-phosphoethanolamine Identifier CHEBI:73004 Charge 0 Formula C21H44NO7P InChIKeyhelp_outline YVYMBNSKXOXSKW-HXUWFJFHSA-N SMILEShelp_outline [C@@H](COC(=O)CCCCCCCCCCCCCCC)(COP(OCC[NH3+])(=O)[O-])O 2D coordinates Mol file for the small molecule Search links Involved in 21 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1-O-hexadecyl-sn-glycero-3-phosphocholine Identifier CHEBI:64496 Charge 0 Formula C24H52NO6P InChIKeyhelp_outline VLBPIWYTPAXCFJ-XMMPIXPASA-N SMILEShelp_outline CCCCCCCCCCCCCCCCOC[C@@H](O)COP([O-])(=O)OCC[N+](C)(C)C 2D coordinates Mol file for the small molecule Search links Involved in 19 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1-O-hexadecyl-2-hexadecanoyl-sn-glycero-3-phosphocholine Identifier CHEBI:72744 (CAS: 88587-94-4) help_outline Charge 0 Formula C40H82NO7P InChIKeyhelp_outline WOTHHEHCEYHCFE-LDLOPFEMSA-N SMILEShelp_outline [H][C@@](COCCCCCCCCCCCCCCCC)(COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCCCCCCCCC 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline sn-glycero-3-phosphoethanolamine Identifier CHEBI:143890 Charge 0 Formula C5H14NO6P InChIKeyhelp_outline JZNWSCPGTDBMEW-RXMQYKEDSA-N SMILEShelp_outline O[C@H](CO)COP(=O)([O-])OCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 18 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:63760 | RHEA:63761 | RHEA:63762 | RHEA:63763 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Subcellular localization and lysophospholipase/transacylation activities of human group IVC phospholipase A2 (cPLA2gamma).
Yamashita A., Tanaka K., Kamata R., Kumazawa T., Suzuki N., Koga H., Waku K., Sugiura T.
cPLA2gamma was identified as an ortholog of cPLA2alpha, which is a key enzyme in eicosanoid production. cPLA2gamma was reported to be located in endoplasmic reticulum (ER) and mitochondria and to have lysophospholipase activity beside phospholipase A2 (PLA2) activity. However, subcellular localiza ... >> More
cPLA2gamma was identified as an ortholog of cPLA2alpha, which is a key enzyme in eicosanoid production. cPLA2gamma was reported to be located in endoplasmic reticulum (ER) and mitochondria and to have lysophospholipase activity beside phospholipase A2 (PLA2) activity. However, subcellular localization, mechanism of membrane binding, regulation and physiological function have not been fully established. In the present study, we examined the subcellular localization and enzymatic properties of cPLA2gamma with C-terminal FLAG-tag. We found that cPLA2gamma was located not only in ER but also mitochondria even in the absence of the prenylation. Purified recombinant cPLA2gamma catalyzed an acyltransferase reaction from one molecule of lysophosphatidylcholine (LPC) to another, forming phosphatidylcholine (PC). LPC or lysophosphatidylethanolamine acted as acyl donor and acceptor, but lysophosphatidylserine, lysophosphatidylinositol and lysophosphatidic acid (LPA) did not. PC and phosphatidylethanolamine (PE) also acted as weak acyl donors. Reaction conditions changed the balance of lysophospholipase and transacylation activities, with addition of LPA/PA, pH>8, and elevated temperature markedly increasing transacylation activity; this suggests that lysophospholipase/transacylation activities of cPLA2gamma may be regulated by various factors. As lysophospholipids are known to accumulate in ischemia heart and to induce arryhthmia, the cPLA2gamma that is abundant in heart may have a protective role through clearance of lysophospholipids by its transacylation activity. << Less
Biochim. Biophys. Acta 1791:1011-1022(2009) [PubMed] [EuropePMC]
This publication is cited by 10 other entries.