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Literature summary for 3.5.1.23 extracted from
- Membrane topology of yeast alkaline ceramidase YPC1 (2013), Biochem. J., 452, 585-594.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene YPC, recombinant expression of HA7-tagged enzyme | Saccharomyces cerevisiae |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G124C | site-directed mutagenesis | Saccharomyces cerevisiae |
| G235C | site-directed mutagenesis | Saccharomyces cerevisiae |
| K157C | site-directed mutagenesis | Saccharomyces cerevisiae |
| K67C | site-directed mutagenesis | Saccharomyces cerevisiae |
| K91C | site-directed mutagenesis | Saccharomyces cerevisiae |
| L65C | site-directed mutagenesis | Saccharomyces cerevisiae |
| additional information | comparison of membrane topology of wild-type and mutant enzymes, overview | Saccharomyces cerevisiae |
| N123C | site-directed mutagenesis | Saccharomyces cerevisiae |
| N158C | site-directed mutagenesis | Saccharomyces cerevisiae |
| R93C | site-directed mutagenesis | Saccharomyces cerevisiae |
| S197C | site-directed mutagenesis | Saccharomyces cerevisiae |
| S293C | site-directed mutagenesis | Saccharomyces cerevisiae |
| S297C | site-directed mutagenesis | Saccharomyces cerevisiae |
| T181C | site-directed mutagenesis | Saccharomyces cerevisiae |
| T98C | site-directed mutagenesis | Saccharomyces cerevisiae |
| V185C | site-directed mutagenesis | Saccharomyces cerevisiae |
| V236C | site-directed mutagenesis | Saccharomyces cerevisiae |
| Y182C | site-directed mutagenesis | Saccharomyces cerevisiae |
| Y184C | site-directed mutagenesis | Saccharomyces cerevisiae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| additional information | the reverse ceramidase activity in microsomes can only be blocked by a lysine residuespecific reagent when the reagent has access to Ypc1p from the lumenal side | Saccharomyces cerevisiae |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| endoplasmic reticulum | - |
Saccharomyces cerevisiae | 5783 | - |
| endoplasmic reticulum | the N- and C-terminal ends of Ypc1p are oriented towards the lumen and cytosol, respectively, cytosolic or lumenal loops | Saccharomyces cerevisiae | 5783 | - |
| membrane | enzyme membrane topology, overview | Saccharomyces cerevisiae | 16020 | - |
| microsome | - |
Saccharomyces cerevisiae | - |
- |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| N-acylsphingosine + H2O | Saccharomyces cerevisiae | the carboxylate is a fatty acid | carboxylate + sphingosine | - |
r |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharomyces cerevisiae | P38298 | gene YPC1 | - |
| Saccharomyces cerevisiae | Q02896 | gene YDC1 | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| N-acylsphingosine + H2O | the carboxylate is a fatty acid | Saccharomyces cerevisiae | carboxylate + sphingosine | - |
r | |
| N-acylsphingosine + H2O | the carboxylate is a fatty acid, Ypc1p can catalyse the reverse reaction, i.e. the condensation of non-esterified fatty acids with phytosphingosine or dihydrosphingosine. The cysteine residues at positions 27 and 219 are required for reverse ceramidase activity | Saccharomyces cerevisiae | carboxylate + sphingosine | - |
r | |
| N-acylsphingosine + H2O | the carboxylate is a fatty acid. The cysteine residues at positions 27 and 219 are required for reverse ceramidase activity | Saccharomyces cerevisiae | carboxylate + sphingosine | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| alkaline ceramidase | - |
Saccharomyces cerevisiae |
| Ydc1p | - |
Saccharomyces cerevisiae |
| yeast dihydroceramidase 1 | - |
Saccharomyces cerevisiae |
| yeast phyto-ceramidase 1 | - |
Saccharomyces cerevisiae |
| Ypc1p | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.4 | - |
assay at | Saccharomyces cerevisiae |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the CREST superfamily | Saccharomyces cerevisiae |
| malfunction | overexpression of Ydc1p protein significantly increases the levels of free long-chain bases and long-chain base-phosphates and reduces the biosynthetic flow of long-chain bases towards mature sphingolipids | Saccharomyces cerevisiae |
| malfunction | overexpression of Ypc1p protein significantly increases the levels of free long-chain bases and long-chain base-phosphates and reduces the biosynthetic flow of long-chain bases towards mature sphingolipids, whereas deletion of gene YPC1 causes a significant increase in mature sphingolipids | Saccharomyces cerevisiae |
| additional information | two of the five natural cysteines, Cys27 and Cys219, are essential for enzymatic activity and form a disulfide bridge. Enzyme Ypc1p possesses the Pfam PF05875 ceramidase motif containing seven predicted transmembranes | Saccharomyces cerevisiae |
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Release 2023.1 (January 2023)
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