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Literature summary extracted from

  • Montes, L.R.; Ibarguren, M.; Goni, F.M.; Stonehouse, M.; Vasil, M.L.; Alonso, A.
    Leakage-free membrane fusion induced by the hydrolytic activity of PlcHR(2), a novel phospholipase C/sphingomyelinase from Pseudomonas aeruginosa (2007), Biochim. Biophys. Acta, 1768, 2365-2372.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.4.3 additional information no effector: Ca2+ in the millimolar range Pseudomonas aeruginosa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
3.1.4.3 Pseudomonas aeruginosa
-
 isoform PlcHR2, bifunctional phospholipase C and sphingomyelinase
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.4.3 additional information the catalytic activity of enyme induces substrate vesicle fusion without relase of vesicular content. The presence of phosphatidylserine in the vesicle composition does not modify significantly enzyme. Induced liposome aggregation, but completely abolishes fusion. Enzyme is inactive on phospholipids that lack choline head groups Pseudomonas aeruginosa ?
-
 ?
3.1.4.3 phosphatidylcholine + H2O phosphatidylcholine and sphingomyelin are cleaved at equal rate Pseudomonas aeruginosa 1,2-diacylglycerol + phosphorylcholine
-
 ?
3.1.4.3 sphingomyelin + H2O phosphatidylcholine and sphingomyelin are cleaved at equal rate Pseudomonas aeruginosa ceramide + phosphorylcholine
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.4.3 PlcHR2
-
 Pseudomonas aeruginosa