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Literature summary for 3.1.4.3 extracted from

  • Urbina, P.; Collado, M.I.; Alonso, A.; Goni, F.M.; Flores-Diaz, M.; Alape-Giron, A.; Ruysschaert, J.M.; Lensink, M.F.
    Unexpected wide substrate specificity of C. perfringens alpha-toxin phospholipase C (2011), Biochim. Biophys. Acta, 1808, 2618-2627.
    View publication on PubMed
Search for more literature for 3.1.4.3

Activating Compound

Activating Compound Comment Organism Structure
cholesterol phospholipase C is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine Clostridium perfringens
additional information no effect on activity by monosialic ganglioside GM3 and phospholipids Clostridium perfringens
phosphatidylethanolamine phospholipase C is enhanced by cholesterol and by lipids with an intrinsic negative curvature, e.g. phosphatidylethanolamine Clostridium perfringens

Cloned(Commentary)

Cloned (Comment) Organism
expression of alpha-toxin in Escherichia coli Clostridium perfringens

Inhibitors

Inhibitors Comment Organism Structure
ganglioside GT1b
-
 Clostridium perfringens
Lysophospholipids
-
 Clostridium perfringens
additional information no effect on activity by monosialic ganglioside GM3 and phospholipids Clostridium perfringens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Clostridium perfringens 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
phosphatidylcholine + H2O Clostridium perfringens
-
 1,2-diacyl-sn-glycerol + choline phosphate
-
 ?
phosphatidylcholine + H2O Clostridium perfringens 8-6
-
 1,2-diacyl-sn-glycerol + choline phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Clostridium perfringens
-
-
-
Clostridium perfringens 8-6
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
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 ?
-
 ?
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 ?
-
 ?
phosphatidylcholine + H2O
-
 Clostridium perfringens 1,2-diacyl-sn-glycerol + choline phosphate
-
 ?
phosphatidylcholine + H2O
-
 Clostridium perfringens 8-6 1,2-diacyl-sn-glycerol + choline phosphate
-
 ?
sphingomyelin + H2O
-
 Clostridium perfringens N-acylsphingosine + choline phosphate
-
 ?
sphingomyelin + H2O
-
 Clostridium perfringens 8-6 N-acylsphingosine + choline phosphate
-
 ?

Synonyms

Synonyms Comment Organism
alpha-toxin
-
 Clostridium perfringens
CpPLC
-
 Clostridium perfringens
phosphatidylcholine phospholipase C
-
 Clostridium perfringens
PLC
-
 Clostridium perfringens

General Information

General Information Comment Organism
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
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
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