Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.4.3 extracted from

  • Ibarguren, M.; Sot, J.; Montes, L.R.; Vasil, A.I.; Vasil, M.L.; Goni, F.M.; Alonso, A.
    Recruitment of a phospholipase C/sphingomyelinase into non-lamellar lipid droplets during hydrolysis of lipid bilayers (2013), Chem. Phys. Lipids, 166, 12-17.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular the enzyme is secreted Pseudomonas aeruginosa
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas aeruginosa PlcHR2 is a secreted toxin that exhibits phospholipase C and sphingomyelinase activities. It shows hydrolytic activity of PlcHR2 on bilayers of varying lipid compositions, e.g. on giant unilamellar vesicles composed of sphingomyelin, phosphatidylcholine, phosphatidylethanolamine, and cholesterol ?
-
?
phosphatidylcholine + H2O Pseudomonas aeruginosa
-
1,2-sn-diacylglycerol + phosphocholine
-
?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information PlcHR2 is a secreted toxin that exhibits phospholipase C and sphingomyelinase activities. It shows hydrolytic activity of PlcHR2 on bilayers of varying lipid compositions, e.g. on giant unilamellar vesicles composed of sphingomyelin, phosphatidylcholine, phosphatidylethanolamine, and cholesterol Pseudomonas aeruginosa ?
-
?
phosphatidylcholine + H2O
-
Pseudomonas aeruginosa 1,2-sn-diacylglycerol + phosphocholine
-
?

Synonyms

Synonyms Comment Organism
phospholipase C/sphingomyelinase
-
Pseudomonas aeruginosa
phospholipase C/sphingomyelinase HR2
-
Pseudomonas aeruginosa
PlcHR2
-
Pseudomonas aeruginosa

General Information

General Information Comment Organism
additional information enzyme binding to lipid vesicles is a slow, cooperative process, but after the initial cluster of bound enzyme molecules further binding and catalytic activity follows rapidly. At some late stage of enzyme activity, apparently three-dimensional structures or lipidic aggregates are formed which marks another burst of enzyme activity, and the lysis of the giant vesicle Pseudomonas aeruginosa
physiological function the enzyme's end-product 1,2-sn-diacylglycerol has an important effect on the bilayer architecture of the lipid membranes/lipid vesicles Pseudomonas aeruginosa