Enzymes
UniProtKB help_outline | 3 proteins |
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- Name help_outline 1-hexadecanoyl-2-nonadioyl-sn-glycero-3-phosphocholine Identifier CHEBI:78207 Charge -1 Formula C33H63NO10P InChIKeyhelp_outline GHQQYDSARXURNG-SSEXGKCCSA-M SMILEShelp_outline CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCC([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 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 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 nonanedioate Identifier CHEBI:78208 Charge -2 Formula C9H14O4 InChIKeyhelp_outline BDJRBEYXGGNYIS-UHFFFAOYSA-L SMILEShelp_outline [O-]C(=O)CCCCCCCC([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
Cross-references
RHEA:41388 | RHEA:41389 | RHEA:41390 | RHEA:41391 | |
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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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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.
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Purification and characterization of bovine brain platelet-activating factor acetylhydrolase.
Hattori M., Arai H., Inoue K.
Platelet-activating factor (PAF) acetylhydrolase, which removes the acetyl moiety at the sn-2 position, has been found in plasma and tissue cytosol. PAF acetylhydrolase in bovine brain cytosol was chromatographically separated into three distinct fractions, all of which exhibited pH optima in the ... >> More
Platelet-activating factor (PAF) acetylhydrolase, which removes the acetyl moiety at the sn-2 position, has been found in plasma and tissue cytosol. PAF acetylhydrolase in bovine brain cytosol was chromatographically separated into three distinct fractions, all of which exhibited pH optima in the neutral to mild alkaline region and were unaffected by EDTA. We have purified the major fraction of the enzyme to near homogeneity. The purified enzyme had a molecular mass of about 100 kDa, as estimated by gel filtration chromatography, and gave three distinct bands of 45, 30, and 29 kDa, respectively, on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. These polypeptides exclusively co-migrated with the activity throughout the purification steps. These data suggest that this set of polypeptides corresponds to the subunits of bovine brain PAF acetylhydrolase. Diisopropyl fluorophosphate completely inhibited the activity at 0.1 mM. [3H]Diisopropyl fluorophosphate labeled only the 29-kDa polypeptide, suggesting that this polypeptide possesses an active serine residue(s). The purified enzyme displayed similar activity against PAF and oxidatively modified phosphatidylcholine, but did not hydrolyze phosphatidylcholine or phosphatidylethanolamine with two long chain acyl groups. Thus, the intracellular PAF acetylhydrolase is likely to be a new member of the calcium-independent phospholipases A2 in mammalian tissues. << Less
J Biol Chem 268:18748-18753(1993) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.