Literature summary for 3.1.4.3 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.

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Activating Compound

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

Organism

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

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	?	-	?
phosphatidylcholine + H2O	phosphatidylcholine and sphingomyelin are cleaved at equal rate	Pseudomonas aeruginosa	1,2-diacylglycerol + phosphorylcholine	-	?
sphingomyelin + H2O	phosphatidylcholine and sphingomyelin are cleaved at equal rate	Pseudomonas aeruginosa	ceramide + phosphorylcholine	-	?

Synonyms

Synonyms	Comment	Organism
PlcHR2	-	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)