Enzymes
| UniProtKB help_outline | 3 proteins |
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- Name help_outline 1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine Identifier CHEBI:74617 Charge -1 Formula C24H45NO9P InChIKeyhelp_outline JZWNYZVVZXZRRH-YFKVPUFHSA-M SMILEShelp_outline CCCCCCCC\C=C/CCCCCCCC(=O)OC[C@@H](O)COP([O-])(=O)OC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 9 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline hexadecanoyl-CoA Identifier CHEBI:57379 Charge -4 Formula C37H62N7O17P3S InChIKeyhelp_outline MNBKLUUYKPBKDU-BBECNAHFSA-J SMILEShelp_outline [C@@H]1(N2C3=C(C(=NC=N3)N)N=C2)O[C@H](COP(OP(OCC(C)([C@H](C(NCCC(NCCSC(CCCCCCCCCCCCCCC)=O)=O)=O)O)C)(=O)[O-])(=O)[O-])[C@H]([C@H]1O)OP([O-])([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 110 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1-(9Z)-octadecenoyl-2-hexadecanoyl-sn-glycero-3-phosphoserine Identifier CHEBI:74909 Charge -1 Formula C40H75NO10P InChIKeyhelp_outline ILJAXXNZNFOOQA-DAQGAKHBSA-M SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)O[C@H](COC(=O)CCCCCCC\C=C/CCCCCCCC)COP([O-])(=O)OC[C@H]([NH3+])C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CoA Identifier CHEBI:57287 (Beilstein: 11604429) help_outline Charge -4 Formula C21H32N7O16P3S InChIKeyhelp_outline RGJOEKWQDUBAIZ-IBOSZNHHSA-J SMILEShelp_outline CC(C)(COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12)[C@@H](O)C(=O)NCCC(=O)NCCS 2D coordinates Mol file for the small molecule Search links Involved in 1,500 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:37415 | RHEA:37416 | RHEA:37417 | RHEA:37418 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils.
Gijon M.A., Riekhof W.R., Zarini S., Murphy R.C., Voelker D.R.
The cycle of deacylation and reacylation of phospholipids plays a critical role in regulating availability of arachidonic acid for eicosanoid production. The major yeast lysophospholipid acyltransferase, Ale1p, is related to mammalian membrane-bound O-acyltransferase (MBOAT) proteins. We expressed ... >> More
The cycle of deacylation and reacylation of phospholipids plays a critical role in regulating availability of arachidonic acid for eicosanoid production. The major yeast lysophospholipid acyltransferase, Ale1p, is related to mammalian membrane-bound O-acyltransferase (MBOAT) proteins. We expressed four human MBOATs in yeast strains lacking Ale1p and studied their acyl-CoA and lysophospholipid specificities using novel mass spectrometry-based enzyme assays. MBOAT1 is a lysophosphatidylserine (lyso-PS) acyltransferase with preference for oleoyl-CoA. MBOAT2 also prefers oleoyl-CoA, using lysophosphatidic acid and lysophosphatidylethanolamine as acyl acceptors. MBOAT5 prefers lysophosphatidylcholine and lyso-PS to incorporate linoleoyl and arachidonoyl chains. MBOAT7 is a lysophosphatidylinositol acyltransferase with remarkable specificity for arachidonoyl-CoA. MBOAT5 and MBOAT7 are particularly susceptible to inhibition by thimerosal. Human neutrophils express mRNA for these four enzymes, and neutrophil microsomes incorporate arachidonoyl chains into phosphatidylinositol, phosphatidylcholine, PS, and phosphatidylethanolamine in a thimerosal-sensitive manner. These results strongly implicate MBOAT5 and MBOAT7 in arachidonate recycling, thus regulating free arachidonic acid levels and leukotriene synthesis in neutrophils. << Less
J. Biol. Chem. 283:30235-30245(2008) [PubMed] [EuropePMC]
This publication is cited by 26 other entries.