Enzymes
UniProtKB help_outline | 6 proteins |
Reaction participants Show >> << Hide
- Name help_outline (9Z)-octadecenoyl-CoA Identifier CHEBI:57387 Charge -4 Formula C39H64N7O17P3S InChIKeyhelp_outline XDUHQPOXLUAVEE-BPMMELMSSA-J SMILEShelp_outline CCCCCCCC\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 103 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-phospho-(1'-sn-glycerol) Identifier CHEBI:72827 Charge -1 Formula C24H48O9P InChIKeyhelp_outline HFJVKBVEKQHVTO-XZOQPEGZSA-M SMILEShelp_outline CCCCCCCCCCCCCCCCCC(=O)OC[C@@H](O)COP([O-])(=O)OC[C@@H](O)CO 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-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-sn-glycerol) Identifier CHEBI:72845 Charge -1 Formula C42H80O10P InChIKeyhelp_outline ZEFGRNLJASLRBZ-QIJYXWHJSA-M SMILEShelp_outline CCCCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OC[C@@H](O)CO)OC(=O)CCCCCCC\C=C/CCCCCCCC 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 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 1,468 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:37647 | RHEA:37648 | RHEA:37649 | RHEA:37650 | |
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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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The microsomal cardiolipin remodeling enzyme acyl-CoA lysocardiolipin acyltransferase is an acyltransferase of multiple anionic lysophospholipids.
Zhao Y., Chen Y.-Q., Li S., Konrad R.J., Cao G.
Phospholipids are subjected to remodeling through the Lands cycle to attain appropriate FA compositions. In recent years, at least two families of lysophospholipid acyltransferases have been identified. Acyl-CoA lysocardiolipin acyltransferase 1 (ALCAT1) was initially identified as a microsomal ly ... >> More
Phospholipids are subjected to remodeling through the Lands cycle to attain appropriate FA compositions. In recent years, at least two families of lysophospholipid acyltransferases have been identified. Acyl-CoA lysocardiolipin acyltransferase 1 (ALCAT1) was initially identified as a microsomal lysocardiolipin acyltransferase. However, the physiological relevance of how this enzyme is involved in cardiolipin remodeling has not been elucidated. We report in this study that ALCAT1 possesses acyltransferase activities toward lysophosphatidylinositol (LPI) and lysophosphatidylglycerol (LPG). Membrane preparations from human embryonic kidney 293 (HEK293) cells overexpressing human ALCAT1 demonstrated significant increases in LPI acyltransferase (LPIAT) and LPG acyltransferase (LPGAT) activities using a variety of fatty acyl-CoAs. The enzyme affinities toward LPI and LPG were determined through kinetic studies suggesting that the LPI binding affinity to ALCAT1 depends on fatty acyl-CoA. Reduced expression of ALCAT1 in Hela cells resulted in significant reductions of LPIAT and LPGAT activities, but not ALCAT activity. Through structural and functional studies, we have identified critical amino acids D168 and L169 within ALCAT1 that are potentially involved in lysophospholipid substrate binding. Our studies provide the molecular basis for future investigations of the physiological function of ALCAT1 and offer evidence of critical amino acids involved in substrate binding for the family of glycerolipid acyltransferases. << Less
J. Lipid Res. 50:945-956(2009) [PubMed] [EuropePMC]
This publication is cited by 13 other entries.
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Molecular identification of a novel mammalian brain isoform of acyl-CoA:lysophospholipid acyltransferase with prominent ethanolamine lysophospholipid acylating activity, LPEAT2.
Cao J., Shan D., Revett T., Li D., Wu L., Liu W., Tobin J.F., Gimeno R.E.
Acyl-CoA-dependent lysophospholipid acyltransferases play an important role in attaining the appropriate molecular species of phospholipids. A number of genes encoding these activities were recently identified. It has become clear that multiple genes can encode one enzymatic activity and that a gi ... >> More
Acyl-CoA-dependent lysophospholipid acyltransferases play an important role in attaining the appropriate molecular species of phospholipids. A number of genes encoding these activities were recently identified. It has become clear that multiple genes can encode one enzymatic activity and that a given gene may encode multiple activities. Here we report the identification of a gene encoding a mammalian acyl-CoA-dependent lysophospholipid acyltransferase with prominent activity toward ethanolamine-containing lysophospholipids, which we termed acyl-CoA:lysophosphatidylethanolamine acyltransferase 2, LPEAT2 (previously annotated as AYTL3 or AGPAT7). LPEAT2 is predominantly expressed in brain, coinciding with an enrichment of phosphatidylethanolamine in this tissue. Ectopic expression of LPEAT2 in mammalian HEK293T cells led to a dramatic increase (up to 9-fold) in LPEAT activity when compared with cells transfected with empty vector or an unrelated acyltransferase. LPEAT2 also exhibited significant acyl-CoA-dependent acyltransferase activity toward 1-O-alkenyl-lysophosphatidylethanolamine, lysophosphatidylglycerol, 1-O-alkyl-lysophosphatidylcholine, lysophosphatidylserine, and lysophosphatidylcholine but lacked appreciable acylating activity toward glycerol 3-phosphate, lysophosphatidic acid, lysophosphatidylinositol, and diacylglycerol, demonstrating multiple but selective functions of LPEAT2 as an enzyme involved in phospholipid remodeling. LPEAT2 recognizes a broad range of medium and long chain fatty acyl-CoA, and its activity was not affected by Ca(2+). When overexpressed in mammalian cells, LPEAT2 is localized to the endoplasmic reticulum. siRNA-mediated knockdown of LPEAT2 in HEK293T cells significantly decreased LPEAT and 1-alkenyl-LPEAT activities but did not affect other lysophospholipid acylating activities. These findings identify LPEAT2 as an important enzyme in the biosynthesis of ethanolamine-containing phospholipids, especially in brain. << Less
J. Biol. Chem. 283:19049-19057(2008) [PubMed] [EuropePMC]
This publication is cited by 18 other entries.