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- Name help_outline 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phospho-L-serine Identifier CHEBI:75032 Charge -1 Formula C42H73NO10P InChIKeyhelp_outline DKLQKRSJZISZKW-KNFJROLASA-M SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OC[C@H]([NH3+])C([O-])=O)OC(=O)CCC\C=C/C\C=C/C\C=C/C\C=C/CCCCC 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 H2O Identifier CHEBI:15377 (Beilstein: 3587155; CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,048 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-phospho-L-serine Identifier CHEBI:77830 Charge -1 Formula C26H43NO9P InChIKeyhelp_outline ITIDLBCKKSNAPK-RRJHOXOUSA-M SMILEShelp_outline CCCCC\C=C/C\C=C/C\C=C/C\C=C/CCCC(=O)O[C@H](CO)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 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 hexadecanoate Identifier CHEBI:7896 (Beilstein: 3589907; CAS: 143-20-4) help_outline Charge -1 Formula C16H31O2 InChIKeyhelp_outline IPCSVZSSVZVIGE-UHFFFAOYSA-M SMILEShelp_outline CCCCCCCCCCCCCCCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 92 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:41187 | RHEA:41188 | RHEA:41189 | RHEA:41190 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Serine phospholipid-specific phospholipase A that is secreted from activated platelets.
Sato T., Aoki J., Nagai Y., Dohmae N., Takio K., Doi T., Arai H., Inoue K.
Rat platelets secrete two types of phospholipases upon stimulation; one is type II phospholipase A2 and the other is serine-phospholipid-selective phospholipase A. In the current study we purified serine-phospholipid-selective phospholipase A and cloned its cDNA. The final preparation, purified fr ... >> More
Rat platelets secrete two types of phospholipases upon stimulation; one is type II phospholipase A2 and the other is serine-phospholipid-selective phospholipase A. In the current study we purified serine-phospholipid-selective phospholipase A and cloned its cDNA. The final preparation, purified from extracellular medium of activated rat platelets, gave a 55-kDa protein band on SDS-polyacrylamide gel electrophoresis. [3H]Diisopropyl fluorophosphate, an inhibitor of the enzyme, labeled the 55-kDa protein, suggesting that this polypeptide possesses active serine residues. The cDNA for the enzyme was cloned from a rat megakaryocyte cDNA library. The predicted 456-amino acid sequence contains a putative short N-terminal signal sequence and a GXSXG sequence, which is a motif of an active serine residue of serine esterase. Amino acid sequence homology analysis revealed that the enzyme shares about 30% homology with mammalian lipases (lipoprotein lipase, hepatic lipase, and pancreatic lipase). Regions surrounding the putative active serine, histidine, and aspartic acid, which may form a "lipase triad," were highly conserved among these enzymes. The recombinant protein, which we expressed in Sf9 insect cells using the baculovirus system, hydrolyzed a fatty acyl residue at the sn-1 position of lysophosphatidylserine and phosphatidylserine, but did not appreciably hydrolyze phosphatidylcholine, phosphatidylethanolamine, phosphatidylinositol, phosphatidic acid, and triglyceride. The present enzyme, named phosphatidylserine-phospholipase A1, is the first phospholipase that exclusively hydrolyses the sn-1 position and has a strict head group specificity for the substrate. << Less
J. Biol. Chem. 272:2192-2198(1997) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.