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Literature summary extracted from
- Bacterial phosphatidylinositol-specific phospholipase C as membrane-attacking agents and tools for research on GPI-anchored proteins (2004), J. Toxicol. Toxin Rev., 23, 479-508.
No PubMed abstract available
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 4.6.1.13 | molecular biology | enzyme is used as a tool in the studies of GPI-anchored proteins | Staphylococcus aureus |
| 4.6.1.13 | molecular biology | enzyme is used as a tool in the studies of GPI-anchored proteins | Bacillus cereus |
| 4.6.1.13 | molecular biology | enzyme is used as a tool in the studies of GPI-anchored proteins | Bacillus thuringiensis |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.6.1.13 | extracellular | - |
Bacillus cereus | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.6.1.13 | additional information | Listeria monocytogenes | the enzyme contributes to listerial infection of epithelial cells and macrophages as a virulence factor cooperating with other factors such as listeriolysin O and phosphatidylcholine-preferring phospholipase C | ? | - |
? |  |
| 4.6.1.13 | additional information | Bacillus thuringiensis | the enzyme exhibits cytotoxicity against some cultivated cells | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.6.1.13 | Bacillus cereus | - |
- |
- |
| 4.6.1.13 | Bacillus thuringiensis | - |
- |
- |
| 4.6.1.13 | Listeria monocytogenes | - |
- |
- |
| 4.6.1.13 | Staphylococcus aureus | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 4.6.1.13 | culture medium | - |
Bacillus cereus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.6.1.13 | additional information | the enzyme contributes to listerial infection of epithelial cells and macrophages as a virulence factor cooperating with other factors such as listeriolysin O and phosphatidylcholine-preferring phospholipase C | Listeria monocytogenes | ? | - |
? | |
| 4.6.1.13 | additional information | the enzyme exhibits cytotoxicity against some cultivated cells | Bacillus thuringiensis | ? | - |
? | |
| 4.6.1.13 | phosphatidylinositol + H2O | at first the enzyme catalyzes phosphate transfer within the molecule of phosphatidylinositol from glycerol OH to 2-OH of myo-inositol, resulting in diacylglycerol and myo-inositol 1,2-cyclic phosphate. Next myo-inositol 1,2-cyclic phosphate is hydrolyzed by the enzyme to inositol 1-phosphate. Since the reaction rate of the first step (phosphotransferase) is 1000 times as much as that of the second step (cyclic phosphodiesterase) myo-inositol 1,2-cyclic phosphate accumulates as one of the major products during enzyme action | Staphylococcus aureus | diacylglycerol + myo-inositol 1,2-cyclic phosphate | - |
? | |
| 4.6.1.13 | phosphatidylinositol + H2O | at first the enzyme catalyzes phosphate transfer within the molecule of phosphatidylinositol from glycerol OH to 2-OH of myo-inositol, resulting in diacylglycerol and myo-inositol 1,2-cyclic phosphate. Next myo-inositol 1,2-cyclic phosphate is hydrolyzed by the enzyme to inositol 1-phosphate. Since the reaction rate of the first step (phosphotransferase) is 1000 times as much as that of the second step (cyclic phosphodiesterase) myo-inositol 1,2-cyclic phosphate accumulates as one of the major products during enzyme action | Listeria monocytogenes | diacylglycerol + myo-inositol 1,2-cyclic phosphate | - |
? | |
| 4.6.1.13 | phosphatidylinositol + H2O | degrades synthetic phosphatidylinositols in the following order dilauroyl > dimyristoly > dioleoyl > dipalmitoyl. At first the enzyme catalyzes phosphate transfer within the molecule of phosphatidylinositol from glycerol OH to 2-OH of myo-inositol, resulting in diacylglycerol and myo-inositol 1,2-cyclic phosphate. Next myo-inositol 1,2-cyclic phosphate is hydrolyzed by the enzyme to inositol 1-phosphate. Since the reaction rate of the first step (phosphotransferase) is 1000 times as much as that of the second step (cyclic phosphodiesterase) myo-inositol 1,2-cyclic phosphate accumulates as one of the major products during enzyme action | Bacillus thuringiensis | diacylglycerol + myo-inositol 1,2-cyclic phosphate | - |
? | |
| 4.6.1.13 | phosphatidylinositol + H2O | at first the enzyme catalyzes phosphate transfer within the molecule of phosphatidylinositol from glycerol OH to 2-OH of myo-inositol, resulting in diacylglycerol and myo-inositol 1,2-cyclic phosphate. Next myo-inositol 1,2-cyclic phosphate is hydrolyzed by the enzyme to inositol 1-phosphate. Since the reaction rate of the first step (phosphotransferase) is 1000 times as much as that of the second step (cyclic phosphodiesterase) myo-inositol 1,2-cyclic phosphate accumulates as one of the major products during enzyme action | Bacillus cereus | diacylglycerol + myo-inositol 1,2-cyclic phosphate + D-myo-inositol 1-phosphate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 4.6.1.13 | phosphatidylinositol-specific phospholipase C | - |
Staphylococcus aureus |
| 4.6.1.13 | phosphatidylinositol-specific phospholipase C | - |
Bacillus cereus |
| 4.6.1.13 | phosphatidylinositol-specific phospholipase C | - |
Listeria monocytogenes |
| 4.6.1.13 | phosphatidylinositol-specific phospholipase C | - |
Bacillus thuringiensis |
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Release 2023.1 (January 2023)
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