Enzymes
| UniProtKB help_outline | 3 proteins |
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- Name help_outline 1-O-alkyl-sn-glycero-3-phosphocholine Identifier CHEBI:30909 Charge 0 Formula C8H19NO6PR SMILEShelp_outline C[N+](C)(C)CCOP([O-])(=O)OC[C@H](O)CO[*] 2D coordinates Mol file for the small molecule Search links Involved in 42 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-O-alkyl-sn-glycero-3-phosphate Identifier CHEBI:58014 Charge -2 Formula C3H6O6PR SMILEShelp_outline O[C@H](CO[*])COP([O-])([O-])=O 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
- Name help_outline choline Identifier CHEBI:15354 (Beilstein: 1736748; CAS: 62-49-7) help_outline Charge 1 Formula C5H14NO InChIKeyhelp_outline OEYIOHPDSNJKLS-UHFFFAOYSA-N SMILEShelp_outline C[N+](C)(C)CCO 2D coordinates Mol file for the small molecule Search links Involved in 56 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:39927 | RHEA:39928 | RHEA:39929 | RHEA:39930 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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New members of the mammalian glycerophosphodiester phosphodiesterase family: GDE4 and GDE7 produce lysophosphatidic acid by lysophospholipase D activity.
Ohshima N., Kudo T., Yamashita Y., Mariggio S., Araki M., Honda A., Nagano T., Isaji C., Kato N., Corda D., Izumi T., Yanaka N.
The known mammalian glycerophosphodiester phosphodiesterases (GP-PDEs) hydrolyze glycerophosphodiesters. In this study, two novel members of the mammalian GP-PDE family, GDE4 and GDE7, were isolated, and the molecular basis of mammalian GP-PDEs was further explored. The GDE4 and GDE7 sequences are ... >> More
The known mammalian glycerophosphodiester phosphodiesterases (GP-PDEs) hydrolyze glycerophosphodiesters. In this study, two novel members of the mammalian GP-PDE family, GDE4 and GDE7, were isolated, and the molecular basis of mammalian GP-PDEs was further explored. The GDE4 and GDE7 sequences are highly homologous and evolutionarily close. GDE4 is expressed in intestinal epithelial cells, spermatids, and macrophages, whereas GDE7 is particularly expressed in gastro-esophageal epithelial cells. Unlike other mammalian GP-PDEs, GDE4 and GDE7 cannot hydrolyze either glycerophosphoinositol or glycerophosphocholine. Unexpectedly, both GDE4 and GDE7 show a lysophospholipase D activity toward lysophosphatidylcholine (lyso-PC). We purified the recombinant GDE4 and GDE7 proteins and show that these enzymes can hydrolyze lyso-PC to produce lysophosphatidic acid (LPA). Further characterization of purified recombinant GDE4 showed that it can also convert lyso-platelet-activating factor (1-O-alkyl-sn-glycero-3-phosphocholine; lyso-PAF) to alkyl-LPA. These data contribute to our current understanding of mammalian GP-PDEs and of their physiological roles via the control of lyso-PC and lyso-PAF metabolism in gastrointestinal epithelial cells and macrophages. << Less
J. Biol. Chem. 290:4260-4271(2015) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
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Studies of lysophospholipase D of rat liver and other tissues.
Wykle R.L., Kraemer W.F., Schremmer J.M.
Arch Biochem Biophys 184:149-155(1977) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.