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

BRENDA support

Literature summary for 3.1.4.12 extracted from

  • Montes, L.-R.; Lopez, D.J.; Sot, J.; Bagatolli, L.A.; Stonehouse, M.J.; Vasil, M.L.; Wu, B.X.; Hannun, Y.A.; Goni, F.M.; Alonso, A.
    Ceramide-enriched membrane domains in red blood cells and the mechanism of sphingomyelinase-induced hot-cold hemolysis (2008), Biochemistry, 47, 11222-11230.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.4.12

Inhibitors

Inhibitors Comment Organism Structure
additional information ceramidase inhibits hot-cold hemolysis induced by PlcHRx2, Cer is essential in the mechanism of hot-cold hemolysis Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas aeruginosa The sphingomyelinase, but not the phospholipase C activity, is essential for induction of hot-cold hemolysis in human erythrocytes, that contain both phosphatidylcholine and sphingomyelin but also in goat erythrocytes, which lack phosphatidylcholine, however, in horse erythrocytes, with a large proportion of phosphatidylcholine and almost no sphingomyelin, hot-cold hemolysis induced by PlcHR2 is not observed, overview. Sphingomyelinase activity gives rise to the formation of ceramide-rich, rigid membrane domains that are resistant to Triton X-100 solubilization ?
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information The sphingomyelinase, but not the phospholipase C activity, is essential for induction of hot-cold hemolysis in human erythrocytes, that contain both phosphatidylcholine and sphingomyelin but also in goat erythrocytes, which lack phosphatidylcholine, however, in horse erythrocytes, with a large proportion of phosphatidylcholine and almost no sphingomyelin, hot-cold hemolysis induced by PlcHR2 is not observed, overview. Sphingomyelinase activity gives rise to the formation of ceramide-rich, rigid membrane domains that are resistant to Triton X-100 solubilization Pseudomonas aeruginosa ?
-
 ?
additional information PlcHR2 toxin from Pseudomonas aeruginosa is an enzyme with both phospholipase C and sphingomyelinase activities, PlcHR2 hydrolyzes phosphatidylcholine and sphingomyelin at similar rates, but other phospholipids are cleaved at much lower rates, if at all Pseudomonas aeruginosa ?
-
 ?
phosphatidylcholine + H2O
-
 Pseudomonas aeruginosa diacylglycerol + choline phosphate
-
 ?
sphingomyelin + H2O
-
 Pseudomonas aeruginosa N-acylsphingosine + choline phosphate
-
 ?

Synonyms

Synonyms Comment Organism
More cf. EC 3.1.4.3, the enzyme is the prototype of another phosphatase superfamily Pseudomonas aeruginosa
phospholipase C/sphingomyelinase
-
 Pseudomonas aeruginosa
PlcHR2
-
 Pseudomonas aeruginosa
PlcHR2 a phospholipase C/sphingomyelinase, the sphingomyelinase, but not the phospholipase C activity, is essential for hot-cold hemolysis Pseudomonas aeruginosa
PlcHR2 toxin
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 hemolysis assay at Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
-
 hemolysis assay at Pseudomonas aeruginosa