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- Name help_outline 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine Identifier CHEBI:74965 Charge 0 Formula C46H84NO8P InChIKeyhelp_outline PSVRFUPOQYJOOZ-QNPWAGBNSA-N SMILEShelp_outline O=C(CCC/C=C\C/C=C\C/C=C\C/C=C\CCCCC)O[C@@H](COP(OCC[N+](C)(C)C)(=O)[O-])COC(=O)CCCCCCCCCCCCCCCCC 2D coordinates Mol file for the small molecule Search links Involved in 8 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline N-(acetyl)-sphing-4-enine Identifier CHEBI:46979 (CAS: 3102-57-6) help_outline Charge 0 Formula C20H39NO3 InChIKeyhelp_outline BLTCBVOJNNKFKC-QUDYQQOWSA-N SMILEShelp_outline CCCCCCCCCCCCC\C=C\[C@@H](O)[C@H](CO)NC(C)=O 2D coordinates Mol file for the small molecule Search links Involved in 38 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 1-octadecanoyl-N-(acetyl)-sphing-4-enine Identifier CHEBI:76074 Charge 0 Formula C38H73NO4 InChIKeyhelp_outline GQVQVSKCUMRWET-PQCGLYSKSA-N SMILEShelp_outline CCCCCCCCCCCCCCCCCC(=O)OC[C@H](NC(C)=O)[C@H](O)\C=C\CCCCCCCCCCCCC 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine Identifier CHEBI:76079 Charge 0 Formula C28H50NO7P InChIKeyhelp_outline IGJKYDBBINVMLH-JXRLJXCWSA-N SMILEShelp_outline CCCCC\C=C/C\C=C/C\C=C/C\C=C/CCCC(=O)O[C@H](CO)COP([O-])(=O)OCC[N+](C)(C)C 2D coordinates Mol file for the small molecule Search links Involved in 14 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:57120 | RHEA:57121 | RHEA:57122 | RHEA:57123 | |
|---|---|---|---|---|
| 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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Determinants of pH profile and acyl chain selectivity in lysosomal phospholipase A2.
Hinkovska-Galcheva V., Kelly R., Manthei K.A., Bouley R., Yuan W., Schwendeman A., Tesmer J.J.G., Shayman J.A.
Lysosomal phospholipase A2 (LPLA<sub>2</sub>) is characterized by broad substrate recognition, peak activity at acidic pH, and the transacylation of lipophilic alcohols, especially <i>N</i>-acetyl-sphingosine. Prior structural analysis of LPLA<sub>2</sub> revealed the presence of an atypical acidi ... >> More
Lysosomal phospholipase A2 (LPLA<sub>2</sub>) is characterized by broad substrate recognition, peak activity at acidic pH, and the transacylation of lipophilic alcohols, especially <i>N</i>-acetyl-sphingosine. Prior structural analysis of LPLA<sub>2</sub> revealed the presence of an atypical acidic residue, Asp13, in the otherwise hydrophobic active site cleft. We hypothesized that Asp13 contributed to the pH profile and/or substrate preference of LPLA<sub>2</sub> for unsaturated acyl chains. To test this hypothesis, we substituted Asp13 for alanine, cysteine, or phenylalanine; then, we monitored the formation of 1-<i>O</i>-acyl-<i>N</i>-acetylsphingosine to measure the hydrolysis of <i>sn</i>-1 versus <i>sn</i>-2 acyl groups on a variety of glycerophospholipids. Substitutions with Asp13 yielded significant enzyme activity at neutral pH (7.4) and perturbed the selectivity for mono- and double-unsaturated acyl chains. However, this position played no apparent role in selecting for either the acyl acceptor or the head group of the glycerophospholipid. Our modeling indicates that Asp13 and its substitutions contribute to the pH activity profile of LPLA<sub>2</sub> and to acyl chain selectivity by forming part of a hydrophobic track occupied by the scissile acyl chain. << Less
J. Lipid Res. 59:1205-1218(2018) [PubMed] [EuropePMC]
This publication is cited by 22 other entries.