Enzymes
UniProtKB help_outline | 270 proteins |
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- Name help_outline 1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine Identifier CHEBI:77890 Charge 0 Formula C29H56NO9P InChIKeyhelp_outline RKIDALSACBQVTN-HHHXNRCGSA-N SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCC=O 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 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 5-oxopentanoate Identifier CHEBI:16120 Charge -1 Formula C5H7O3 InChIKeyhelp_outline VBKPPDYGFUZOAJ-UHFFFAOYSA-M SMILEShelp_outline [H]C(=O)CCCC([O-])=O 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 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:40483 | RHEA:40484 | RHEA:40485 | RHEA:40486 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Release of free F2-isoprostanes from esterified phospholipids is catalyzed by intracellular and plasma platelet-activating factor acetylhydrolases.
Stafforini D.M., Sheller J.R., Blackwell T.S., Sapirstein A., Yull F.E., McIntyre T.M., Bonventre J.V., Prescott S.M., Roberts L.J. II
F2-isoprostanes are produced in vivo by nonenzymatic peroxidation of arachidonic acid esterified in phospholipids. Increased urinary and plasma F2-isoprostane levels are associated with a number of human diseases. These metabolites are regarded as excellent markers of oxidant stress in vivo. Isopr ... >> More
F2-isoprostanes are produced in vivo by nonenzymatic peroxidation of arachidonic acid esterified in phospholipids. Increased urinary and plasma F2-isoprostane levels are associated with a number of human diseases. These metabolites are regarded as excellent markers of oxidant stress in vivo. Isoprostanes are initially generated in situ, i.e. when the arachidonate precursor is esterified in phospholipids, and they are subsequently released in free form. Although the mechanism(s) responsible for the release of free isoprostanes after in situ generation in membrane phospholipids is, for the most part, unknown, this process is likely mediated by phospholipase A2 activity(ies). Here we reported that human plasma contains an enzymatic activity that catalyzes this reaction. The activity associates with high density and low density lipoprotein and comigrates with platelet-activating factor (PAF) acetylhydrolase on KBr density gradients. Plasma samples from subjects deficient in PAF acetylhydrolase do not release F2-isoprostanes from esterified precursors. The intracellular PAF acetylhydrolase II, which shares homology to the plasma enzyme, also catalyzes this reaction. We found that both the intracellular and plasma PAF acetylhydrolases have high affinity for esterified F2-isoprostanes. However, the rate of esterified F2-isoprostane hydrolysis is much slower compared with the rate of hydrolysis of other substrates utilized by these enzymes. Studies using PAF acetylhydrolase transgenic mice indicated that these animals have a higher capacity to release F2-isoprostanes compared with nontransgenic littermates. Our results suggested that PAF acetylhydrolases play key roles in the hydrolysis of F2-isoprostanes esterified on phospholipids in vivo. << Less
J. Biol. Chem. 281:4616-4623(2006) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Metabolomics annotates ABHD3 as a physiologic regulator of medium-chain phospholipids.
Long J.Z., Cisar J.S., Milliken D., Niessen S., Wang C., Trauger S.A., Siuzdak G., Cravatt B.F.
All organisms, including humans, possess a huge number of uncharacterized enzymes. Here we describe a general cell-based screen for enzyme substrate discovery by untargeted metabolomics and its application to identify the protein α/β-hydrolase domain-containing 3 (ABHD3) as a lipase that selective ... >> More
All organisms, including humans, possess a huge number of uncharacterized enzymes. Here we describe a general cell-based screen for enzyme substrate discovery by untargeted metabolomics and its application to identify the protein α/β-hydrolase domain-containing 3 (ABHD3) as a lipase that selectively cleaves medium-chain and oxidatively truncated phospholipids. Abhd3(-/-) mice possess elevated myristoyl (C14)-phospholipids, including the bioactive lipid C14-lysophosphatidylcholine, confirming the physiological relevance of our substrate assignments. << Less
Nat. Chem. Biol. 7:763-765(2011) [PubMed] [EuropePMC]
This publication is cited by 18 other entries.