Reaction participants Show >> << Hide
- Name help_outline a 1,2-diacyl-sn-glycero-3-phosphocholine Identifier CHEBI:57643 Charge 0 Formula C10H18NO8PR2 SMILEShelp_outline [C@](COC(=O)*)(OC(=O)*)([H])COP(OCC[N+](C)(C)C)([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 315 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1,2-diacyl-sn-glycero-3-phosphoethanolamine Identifier CHEBI:64612 Charge 0 Formula C7H12NO8PR2 SMILEShelp_outline O(P(=O)(OCC[NH3+])[O-])C[C@H](OC(*)=O)COC(*)=O 2D coordinates Mol file for the small molecule Search links Involved in 132 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1-acyl-sn-glycero-3-phosphocholine Identifier CHEBI:58168 Charge 0 Formula C9H19NO7PR SMILEShelp_outline C[N+](C)(C)CCOP([O-])(=O)OC[C@H](O)COC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 213 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-acyl-1,2-diacyl-sn-glycero-3-phosphoethanolamine Identifier CHEBI:62537 Charge -1 Formula C8H10NO9PR3 SMILEShelp_outline [O-]P(=O)(OCCNC([*])=O)OC[C@@H](COC([*])=O)OC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 32 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:45192 | RHEA:45193 | RHEA:45194 | RHEA:45195 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
Specific form(s) of this reaction
More general form(s) of this reaction
Publications
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Characterization of the human tumor suppressors TIG3 and HRASLS2 as phospholipid-metabolizing enzymes.
Uyama T., Jin X.H., Tsuboi K., Tonai T., Ueda N.
Tazarotene-induced protein 3 (TIG3) and HRAS-like suppressor family 2 (HRASLS2) exhibit tumor-suppressing activities and belong to the lecithin retinol acyltransferase (LRAT) protein family. Since Ca(2+)-independent N-acyltransferase and H-rev107 (another tumor suppressor), both of which are membe ... >> More
Tazarotene-induced protein 3 (TIG3) and HRAS-like suppressor family 2 (HRASLS2) exhibit tumor-suppressing activities and belong to the lecithin retinol acyltransferase (LRAT) protein family. Since Ca(2+)-independent N-acyltransferase and H-rev107 (another tumor suppressor), both of which are members of the LRAT family, have been recently reported to possess catalytic activities related to phospholipid metabolism, we examined possible enzyme activities of human TIG3 and HRASLS2 together with human H-rev107. The purified recombinant proteins of TIG3, HRASLS2, and H-rev107 functioned as phospholipase (PL) A(1/2) in a Ca(2+)-independent manner with maximal activities of 0.53, 0.67, and 2.57 micromol/min/mg of protein, respectively. The proteins were active with various phosphatidylcholines (PCs) and phosphatidylethanolamines (PEs), and for most of substrates the PLA(1) activity was much higher than the PLA(2) activity. In addition, HRASLS2 catalyzed N-acylation of PE to form N-acyl-PE and O-acylation of lyso PC to form PC. TIG3 and H-rev107 catalyzed the N-acylation and O-acylation at relatively low rates. Moreover, these three proteins showed different expression profiles in human tissues. These results suggest that the tumor suppressors TIG3, HRASLS2 and H-rev107 are involved in the phospholipid metabolism with different physiological roles. << Less
Biochim. Biophys. Acta 1791:1114-1124(2009) [PubMed] [EuropePMC]
This publication is cited by 13 other entries.