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Literature summary extracted from
- Unexpected wide substrate specificity of C. perfringens alpha-toxin phospholipase C (2011), Biochim. Biophys. Acta, 1808, 2618-2627.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.4.3 | cholesterol | phospholipase C is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine | Clostridium perfringens |  |
| 3.1.4.3 | additional information | no effect on activity by monosialic ganglioside GM3 and phospholipids | Clostridium perfringens | |
| 3.1.4.3 | phosphatidylethanolamine | phospholipase C is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine | Clostridium perfringens | |
| 3.1.4.12 | cholesterol | sphingomyelinase is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine | Clostridium perfringens | |
| 3.1.4.12 | additional information | no effect on activity by monosialic ganglioside GM3 and phospholipids | Clostridium perfringens | |
| 3.1.4.12 | phosphatidylethanolamine | sphingomyelinase is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine | Clostridium perfringens | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.4.3 | expression of alpha-toxin in Escherichia coli | Clostridium perfringens |
| 3.1.4.12 | expression of alpha-toxin in Escherichia coli | Clostridium perfringens |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.4.3 | ganglioside GT1b | - |
Clostridium perfringens | |
| 3.1.4.3 | Lysophospholipids | - |
Clostridium perfringens | |
| 3.1.4.3 | additional information | no effect on activity by monosialic ganglioside GM3 and phospholipids | Clostridium perfringens | |
| 3.1.4.12 | ganglioside GT1b | - |
Clostridium perfringens | |
| 3.1.4.12 | Lysophospholipids | - |
Clostridium perfringens | |
| 3.1.4.12 | additional information | no effect on activity by monosialic ganglioside GM3 and phospholipids | Clostridium perfringens |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.1.4.3 | membrane | - |
Clostridium perfringens | 16020 | - |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.4.3 | phosphatidylcholine + H2O | Clostridium perfringens | - |
1,2-diacyl-sn-glycerol + choline phosphate | - |
? | |
| 3.1.4.3 | phosphatidylcholine + H2O | Clostridium perfringens 8-6 | - |
1,2-diacyl-sn-glycerol + choline phosphate | - |
? | |
| 3.1.4.12 | a sphingomyelin + H2O | Clostridium perfringens | - |
a ceramide + choline phosphate | - |
? | |
| 3.1.4.12 | a sphingomyelin + H2O | Clostridium perfringens 8-6 | - |
a ceramide + choline phosphate | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.4.3 | Clostridium perfringens | - |
- |
- |
| 3.1.4.3 | Clostridium perfringens 8-6 | - |
- |
- |
| 3.1.4.12 | Clostridium perfringens | - |
- |
- |
| 3.1.4.12 | Clostridium perfringens 8-6 | - |
- |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.4.3 | additional information | substrate specificity analysis by molecular docking reveals that the enzyme is also active with phosphatidylethanolamine and phosphatidylinositol, and to a lower level with phosphatidylglycerol, overview | Clostridium perfringens | ? | - |
? | |
| 3.1.4.3 | additional information | substrate specificity analysis by molecular docking reveals that the enzyme is also active with phosphatidylethanolamine and phosphatidylinositol, and to a lower level with phosphatidylglycerol, overview | Clostridium perfringens 8-6 | ? | - |
? | |
| 3.1.4.3 | phosphatidylcholine + H2O | - |
Clostridium perfringens | 1,2-diacyl-sn-glycerol + choline phosphate | - |
? | |
| 3.1.4.3 | phosphatidylcholine + H2O | - |
Clostridium perfringens 8-6 | 1,2-diacyl-sn-glycerol + choline phosphate | - |
? | |
| 3.1.4.3 | sphingomyelin + H2O | - |
Clostridium perfringens | N-acylsphingosine + choline phosphate | - |
? | |
| 3.1.4.3 | sphingomyelin + H2O | - |
Clostridium perfringens 8-6 | N-acylsphingosine + choline phosphate | - |
? | |
| 3.1.4.12 | a sphingomyelin + H2O | - |
Clostridium perfringens | a ceramide + choline phosphate | - |
? | |
| 3.1.4.12 | a sphingomyelin + H2O | - |
Clostridium perfringens 8-6 | a ceramide + choline phosphate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.4.3 | alpha-toxin | - |
Clostridium perfringens |
| 3.1.4.3 | CpPLC | - |
Clostridium perfringens |
| 3.1.4.3 | phosphatidylcholine phospholipase C | - |
Clostridium perfringens |
| 3.1.4.3 | PLC | - |
Clostridium perfringens |
| 3.1.4.12 | alpha-toxin | - |
Clostridium perfringens |
| 3.1.4.12 | SMase | - |
Clostridium perfringens |
| 3.1.4.12 | sphingomyelinase | - |
Clostridium perfringens |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.4.3 | additional information | establishing enzyme activity in lipid vesicles, method development, overview. Both lipase activities are sensitive to vesicle size, but in opposite ways: while phospholipase C is higher with larger vesicles, sphingomyelinase activity is lower | Clostridium perfringens |
| 3.1.4.3 | physiological function | alpha-toxin, a major determinant of Clostridium perfringens toxicity, exhibits both phospholipase C and sphingomyelinase, EC 3.1.4.12, activities with distinct, but partially overlapping and interacting active sites | Clostridium perfringens |
| 3.1.4.3 | physiological function | the lipase activity serves the bacteriumto generate lipid signals in the host eukaryotic cell, and ultimately to degrade the host cellmembranes, and is the main virulence factor for gas gangrene in humans | Clostridium perfringens |
| 3.1.4.12 | additional information | establishing enzyme activity in lipid vesicles, method development, overview. Both lipase activities are sensitive to vesicle size, but in opposite ways: while phospholipase C is higher with larger vesicles, sphingomyelinase activity is lower | Clostridium perfringens |
| 3.1.4.12 | physiological function | alpha-toxin, a major determinant of Clostridium perfringens toxicity, exhibits both phospholipase C and sphingomyelinase activities with distinct, but partially overlapping and interacting active sites | Clostridium perfringens |
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