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- 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 276 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) Identifier CHEBI:57880 Charge -1 Formula C11H16O13PR2 SMILEShelp_outline [C@@H]1([C@@H]([C@@H]([C@@H]([C@H]([C@@H]1O)O)O)O)OP(OC[C@@H](COC(=O)*)OC(=O)*)(=O)[O-])O 2D coordinates Mol file for the small molecule Search links Involved in 71 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline an inositol-1-phosphoceramide Identifier CHEBI:64916 Charge -1 Formula C10H17NO11PR2 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)NC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 33 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 1,2-diacyl-sn-glycerol Identifier CHEBI:17815 Charge 0 Formula C5H6O5R2 SMILEShelp_outline OC[C@@H](COC([*])=O)OC([*])=O 2D coordinates Mol file for the small molecule Search links Involved in 196 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:55588 | RHEA:55589 | RHEA:55590 | RHEA:55591 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Inhibition of yeast inositol phosphorylceramide synthase by aureobasidin A measured by a fluorometric assay.
Zhong W., Murphy D.J., Georgopapadakou N.H.
Inositol phosphorylceramide synthase (IPC synthase) is an essential and unique enzyme in fungal sphingolipid biosynthesis and is the target of the cyclic nonadepsipeptide antibiotic aureobasidin A. As a first step towards understanding the mechanism of aureobasidin A inhibition, we developed a flu ... >> More
Inositol phosphorylceramide synthase (IPC synthase) is an essential and unique enzyme in fungal sphingolipid biosynthesis and is the target of the cyclic nonadepsipeptide antibiotic aureobasidin A. As a first step towards understanding the mechanism of aureobasidin A inhibition, we developed a fluorometric HPLC assay for IPC synthase using the Saccharomyces cerevisiae enzyme and the fluorescent substrate analog 6-[N-(7-nitro-2,1, 3-benzoxadiazol-4-yl)amino]-hexanoyl ceramide (C(6)-NBD-cer). The kinetic parameters for C(6)-NBD-cer were comparable to those for the synthetic substrate N-acetylsphinganine used previously. Aureobasidin A acted as a tight-binding, non-competitive inhibitor with respect to C(6)-NBD-cer and had a K(i) of 0.55 nM. << Less
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Inositol phosphorylceramide synthase is located in the Golgi apparatus of Saccharomyces cerevisiae.
Levine T.P., Wiggins C.A., Munro S.
The plasma membrane of eukaryotic cells differs in lipid composition from most of the internal organelles, presumably reflecting differences in many of its functions. In particular, the plasma membrane is rich in sphingolipids and sterols, one property of which is to decrease the permeability and ... >> More
The plasma membrane of eukaryotic cells differs in lipid composition from most of the internal organelles, presumably reflecting differences in many of its functions. In particular, the plasma membrane is rich in sphingolipids and sterols, one property of which is to decrease the permeability and increase the thickness of lipid bilayers. In this paper, we examine the length of transmembrane domains throughout the yeast secretory pathway. Although the transmembrane domains of cis and medial Golgi residents are similar to those of endoplasmic reticulum proteins, these domains lengthen substantially beyond the medial Golgi, suggesting a thickening of the bilayer. Yeast sphingolipids have particularly long acyl chains, and Aur1p, the inositol phosphorylceramide synthase that initiates yeast sphingolipid synthesis, was found to be located in the Golgi apparatus by both immunofluorescence and membrane fractionation, with its active site apparently in the Golgi lumen. Thus, it appears that sphingolipid synthesis in yeast takes place in the Golgi, separated from glycerophospholipid synthesis in the endoplasmic reticulum. A similar separation has been found in mammalian cells, and this conservation suggests that such an arrangement of enzymes within the secretory pathway could be important for the creation of bilayers of different thickness within the cell. << Less
Mol. Biol. Cell 11:2267-2281(2000) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.