Enzymes
| UniProtKB help_outline | 2 proteins |
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- Name help_outline (9Z,12Z,15Z)-octadecatrienoyl-CoA Identifier CHEBI:74034 Charge -4 Formula C39H60N7O17P3S InChIKeyhelp_outline OMKFKBGZHNJNEX-PQBHNYBOSA-J SMILEShelp_outline CC\C=C/C\C=C/C\C=C/CCCCCCCC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(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 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline sn-glycerol 3-phosphocholine Identifier CHEBI:16870 (Beilstein: 6062450; CAS: 28319-77-9) help_outline Charge 0 Formula C8H20NO6P InChIKeyhelp_outline SUHOQUVVVLNYQR-MRVPVSSYSA-N SMILEShelp_outline C[N+](C)(C)CCOP([O-])(=O)OC[C@H](O)CO 2D coordinates Mol file for the small molecule Search links Involved in 42 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (9Z,12Z,15Z-octadecatrienoyl)-sn-glycero-3-phosphocholine Identifier CHEBI:140445 Charge 0 Formula C26H48NO7P SMILEShelp_outline [C@](CO*)(O*)([H])COP(OCC[N+](C)(C)C)(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 2 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 1,511 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:56164 | RHEA:56165 | RHEA:56166 | RHEA:56167 | |
|---|---|---|---|---|
| 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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Cloning of glycerophosphocholine acyltransferase (GPCAT) from fungi and plants: a novel enzyme in phosphatidylcholine synthesis.
Glab B., Beganovic M., Anaokar S., Hao M.S., Rasmusson A.G., Patton-Vogt J., Banas A., Stymne S., Lager I.
Glycero-3-phosphocholine (GPC), the product of the complete deacylation of phosphatidylcholine (PC), was long thought to not be a substrate for reacylation. However, it was recently shown that cell-free extracts from yeast and plants could acylate GPC with acyl groups from acyl-CoA. By screening e ... >> More
Glycero-3-phosphocholine (GPC), the product of the complete deacylation of phosphatidylcholine (PC), was long thought to not be a substrate for reacylation. However, it was recently shown that cell-free extracts from yeast and plants could acylate GPC with acyl groups from acyl-CoA. By screening enzyme activities of extracts derived from a yeast knock-out collection, we were able to identify and clone the yeast gene (GPC1) encoding the enzyme, named glycerophosphocholine acyltransferase (GPCAT). By homology search, we also identified and cloned GPCAT genes from three plant species. All enzymes utilize acyl-CoA to acylate GPC, forming lyso-PC, and they show broad acyl specificities in both yeast and plants. In addition to acyl-CoA, GPCAT efficiently utilizes LPC and lysophosphatidylethanolamine as acyl donors in the acylation of GPC. GPCAT homologues were found in the major eukaryotic organism groups but not in prokaryotes or chordates. The enzyme forms its own protein family and does not contain any of the acyl binding or lipase motifs that are present in other studied acyltransferases and transacylases. In vivo labeling studies confirm a role for Gpc1p in PC biosynthesis in yeast. It is postulated that GPCATs contribute to the maintenance of PC homeostasis and also have specific functions in acyl editing of PC (e.g. in transferring acyl groups modified at the sn-2 position of PC to the sn-1 position of this molecule in plant cells). << Less
J. Biol. Chem. 291:25066-25076(2016) [PubMed] [EuropePMC]
This publication is cited by 11 other entries.