Enzymes
UniProtKB help_outline | 2 proteins |
Reaction participants Show >> << Hide
- 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-octadecanoyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphoethanolamine Identifier CHEBI:78268 Charge 0 Formula C43H78NO8P InChIKeyhelp_outline ANRKEHNWXKCXDB-BHFWLYLHSA-N SMILEShelp_outline CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[NH3+])OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine Identifier CHEBI:55430 (Beilstein: 7242477; CAS: 86288-11-1) help_outline Charge 0 Formula C44H82NO7P InChIKeyhelp_outline DUUSFCFZBREELS-WWBBCYQPSA-N SMILEShelp_outline P(OC[C@@H](COCCCCCCCCCCCCCCCC)OC(CCC/C=C\C/C=C\C/C=C\C/C=C\CCCCC)=O)(=O)(OCC[N+](C)(C)C)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1-octadecanoyl-sn-glycero-3-phosphoethanolamine Identifier CHEBI:75036 Charge 0 Formula C23H48NO7P InChIKeyhelp_outline BBYWOYAFBUOUFP-JOCHJYFZSA-N SMILEShelp_outline CCCCCCCCCCCCCCCCCC(=O)OC[C@@H](O)COP([O-])(=O)OCC[NH3+] 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:63776 | RHEA:63777 | RHEA:63778 | RHEA:63779 | |
---|---|---|---|---|
Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
|
Publications
-
Roles of C-terminal processing, and involvement in transacylation reaction of human group IVC phospholipase A2 (cPLA2gamma).
Yamashita A., Kamata R., Kawagishi N., Nakanishi H., Suzuki H., Sugiura T., Waku K.
The phospholipase A2s (PLA2s) are a diverse group of enzymes that hydrolyze the sn-2 fatty acid from phospholipids and play a role in a wide range of physiological functions. A 61-kDa calcium-independent PLA2, termed cPLA2gamma, was identified as an ortholog of cPLA2alpha with approximately 30% ov ... >> More
The phospholipase A2s (PLA2s) are a diverse group of enzymes that hydrolyze the sn-2 fatty acid from phospholipids and play a role in a wide range of physiological functions. A 61-kDa calcium-independent PLA2, termed cPLA2gamma, was identified as an ortholog of cPLA2alpha with approximately 30% overall sequence identity. cPLA2gamma contains a potential prenylation motif at its C terminus, and is known to have PLA2 and lysophospholipase activities, but its physiological roles have not been clarified. In the present study, we expressed various forms of recombinant cPLA2gamma, including non-prenylated and non-cleaved forms, in order to investigate the effects of C-terminal processing. We examined the expression of the wild type and non-prenylated (SCLA) forms of cPLA2gamma, and found that the SCLA form was expressed normally and retained almost full activity. Expression of the prenylated and non-cleaved form of cPLA2gamma using yeast mutants lacking prenyl protein proteases AFC1 (a-factor-converting enzyme) and RCE1 (Ras-converting enzyme) revealed decreased expression in the mutant strain compared to that in the wild type yeast, suggesting that complete C-terminal processing is important for the functional expression of cPLA2gamma. In addition, cPLA2gamma was found to have coenzyme A (CoA)-independent transacylation and lysophospholipid (LPL) dismutase (LPLase/transacylase) activities, suggesting that it may be involved in fatty acid remodeling of phospholipids and the clearance of toxic lysophospholipids in cells. << Less
J. Biochem. 137:557-567(2005) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
-
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.