Enzymes
| UniProtKB help_outline | 267 proteins |
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- Name help_outline 1-hexadecanoyl-2-(10-hydroperoxy-8E-octadecenoyl)-sn-glycero-3-phosphocholine Identifier CHEBI:77749 Charge 0 Formula C42H82NO10P InChIKeyhelp_outline WDVMUQGXOAZRKX-JLMWPCEGSA-N SMILEShelp_outline [H][C@@](COC(=O)CCCCCCCCCCCCCCC)(COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCC\C=C\C(CCCCCCCC)OO 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 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 1-hexadecanoyl-sn-glycero-3-phosphocholine Identifier CHEBI:72998 (CAS: 14863-27-5) help_outline Charge 0 Formula C24H50NO7P InChIKeyhelp_outline ASWBNKHCZGQVJV-HSZRJFAPSA-N SMILEShelp_outline [C@@H](COC(=O)CCCCCCCCCCCCCCC)(COP(OCC[N+](C)(C)C)(=O)[O-])O 2D coordinates Mol file for the small molecule Search links Involved in 77 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 10-hydroperoxy-(8E)-octadecenoate Identifier CHEBI:77755 Charge -1 Formula C18H33O4 InChIKeyhelp_outline HTIQDCPWTUODDW-NTCAYCPXSA-M SMILEShelp_outline CCCCCCCCC(OO)\C=C\CCCCCCC([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 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
Cross-references
| RHEA:41155 | RHEA:41156 | RHEA:41157 | RHEA:41158 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Phospholipase action of platelet-activating factor acetylhydrolase, but not paraoxonase-1, on long fatty acyl chain phospholipid hydroperoxides.
Kriska T., Marathe G.K., Schmidt J.C., McIntyre T.M., Girotti A.W.
Phospholipid hydroperoxide (PLOOH) degrading activity of high density lipoprotein (HDL)-derived paraoxonase-1 (PON1) was investigated, using peroxidized 1-palmitoyl-2-oleoyl phosphatidylcholine (PCOOH) as substrate and high performance thin layer chromatography for quantitative peroxide analysis. ... >> More
Phospholipid hydroperoxide (PLOOH) degrading activity of high density lipoprotein (HDL)-derived paraoxonase-1 (PON1) was investigated, using peroxidized 1-palmitoyl-2-oleoyl phosphatidylcholine (PCOOH) as substrate and high performance thin layer chromatography for quantitative peroxide analysis. Incubation of PCOOH with PON1 resulted in decay of the latter and reciprocal buildup of oleic acid hydroperoxide (OAOOH) at rates unaffected by GSH or other reductants. A serine esterase inhibitor blocked this activity and a recombinant PON1 was devoid of it, raising the possibility that the activity represents platelet-activating factor acetylhydrolase (PAF-AH), an esterase that co-purifies with PON1 from HDL. This was verified by showing that a recombinant PAF-AH recapitulates the ability of natural PON1 to hydrolyze PCOOH and release OAOOH while having essentially no effect on parental PC. Furthermore, recombinant PAF-AH and natural PON1 were shown to have similar K(m) values for PCOOH hydrolysis. Finally, we found that recombinant PAF-AH, but not PON1, catalyzes PLOOH hydrolysis in peroxidized low density lipoprotein. We conclude from this study that PON1 is neither a PLOOH peroxidase nor hydrolase and that the phospholipase A(2)-like activity previously attributed to PON1 in natural enzyme preparations was actually due to novel PLOOH hydrolytic activity of contaminating PAF-AH. << Less
J. Biol. Chem. 282:100-108(2007) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.