Lecithinase C Explained
Phospholipase C |
Ec Number: | 3.1.4.3 |
Cas Number: | 9001-86-9 |
Phospholipase C (EC 3.1.4.3, lipophosphodiesterase I, Clostridium welchii α-toxin, Clostridium oedematiens β- and γ-toxins, lipophosphodiesterase C, phosphatidase C, heat-labile hemolysin, α-toxin) is an enzyme with systematic name phosphatidylcholine cholinephosphohydrolase.[1] [2] [3] [4] This enzyme catalyses the following chemical reaction
a phosphatidylcholine + H2O
1,2-diacyl-
sn-glycerol +
phosphocholineThe bacterial enzyme is a zinc protein. It also acts on sphingomyelin and phosphatidylinositol.
Notes and References
- Druzhinina KV, Kritsman MG . [Lecithinase C in animal tissue] . Biokhimiia . 17 . 1 . 77–81 . 1952 . 13066482 .
- Little C, Otnåss AB . The metal ion dependence of phospholipase C from Bacillus cereus . Biochimica et Biophysica Acta (BBA) - Enzymology . 391 . 2 . 326–33 . June 1975 . 807246 . 10.1016/0005-2744(75)90256-9 .
- Sheikhnejad RG, Srivastava PN . Isolation and properties of a phosphatidylcholine-specific phospholipase C from bull seminal plasma . The Journal of Biological Chemistry . 261 . 16 . 7544–9 . June 1986 . 3086312 .
- Takahashi T, Sugahara T, Ohsaka A . Purification of Clostridium perfringens phospholipase C (alpha-toxin) by affinity chromatography on agarose-linked egg-yolk lipoprotein . Biochimica et Biophysica Acta (BBA) - Protein Structure . 351 . 1 . 155–71 . May 1974 . 4365891 . 10.1016/0005-2795(74)90074-9 .