Reaction participants Show >> << Hide
- Name help_outline an α-mannosylinositol-1-phosphoceramide Identifier CHEBI:166921 Charge -1 Formula C16H27NO16PR2 SMILEShelp_outline O[C@H](*)[C@H](COP([O-])(=O)O[C@@H]1[C@H](O)[C@H](O)[C@@H](O)[C@H](O)[C@H]1O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@@H]2O)NC(*)=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 a D-mannosyl-α-1→6-inositol-1-phosphate Identifier CHEBI:167051 Charge -2 Formula C12H21O14P InChIKeyhelp_outline UJXBXUSHOWRLIG-FZUJBOGNSA-L SMILEShelp_outline [O-]P(=O)(O[C@H]1[C@@H]([C@H]([C@@H]([C@H]([C@H]1O)O)O)O)O[C@@H]2[C@H]([C@H]([C@@H]([C@H](O2)CO)O)O)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 an N-acyl-sphingoid base Identifier CHEBI:83273 Charge 0 Formula C4H7NO3R2 SMILEShelp_outline OC[C@H](NC([*])=O)[C@H](O)[*] 2D coordinates Mol file for the small molecule Search links Involved in 263 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:66312 | RHEA:66313 | RHEA:66314 | RHEA:66315 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
|
Related reactions help_outline
More general form(s) of this reaction
Publications
-
Identification of ISC1 (YER019w) as inositol phosphosphingolipid phospholipase C in Saccharomyces cerevisiae.
Sawai H., Okamoto Y., Luberto C., Mao C., Bielawska A., Domae N., Hannun Y.A.
Sphingolipids have emerged as novel bioactive mediators in eukaryotic cells including yeast. It has been proposed that sphingomyelin (SM) hydrolysis and the concomitant generation of ceramide are involved in various stress responses in mammalian cells. The yeast Saccharomyces cerevisiae has inosit ... >> More
Sphingolipids have emerged as novel bioactive mediators in eukaryotic cells including yeast. It has been proposed that sphingomyelin (SM) hydrolysis and the concomitant generation of ceramide are involved in various stress responses in mammalian cells. The yeast Saccharomyces cerevisiae has inositol phosphosphingolipids (IPS) instead of SM and glycolipids, and synthesis of IPS is indispensable to its growth. Although the genes responsible for the synthesis of IPS have been identified, the gene(s) for the degradation of IPS has not been reported. Here we show that ISC1 (YER019w), which has homology to bacterial neutral sphingomyelinase (SMase), encodes IPS phospholipase C (IPS-PLC). First, we observed that overexpression of ISC1 greatly increased neutral SMase activity, and this activity was dependent on the presence of phosphatidylserine. Cells deleted in ISC1 demonstrated negligible neutral SMase activity. Because yeast cells have IPS instead of SM, we investigated whether IPS are the physiologic substrates of this enzyme. Lysates of ISC1-overexpressing cells demonstrated very high PLC activities on IPS. Deletion of ISC1 eliminated endogenous IPS-PLC activities. Labeling yeast cells with [(3)H]dihydrosphingosine showed that IPS were increased in the deletion mutant cells. This study identifies the first enzyme involved in catabolism of complex sphingolipids in S. cerevisiae. << Less
J. Biol. Chem. 275:39793-39798(2000) [PubMed] [EuropePMC]
This publication is cited by 5 other entries.