Lecithinase C
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| Phospholipase C | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.4.3 | ||||||||
| CAS no. | 9001-86-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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 + phosphocholine
The bacterial enzyme is a zinc protein. It also acts on sphingomyelin and phosphatidylinositol.
References
- ^ Druzhinina KV, Kritsman MG (1952). "[Lecithinase C in animal tissue]". Biokhimiia. 17 (1): 77–81. PMID 13066482.
- ^ Little C, Otnåss AB (June 1975). "The metal ion dependence of phospholipase C from Bacillus cereus". Biochimica et Biophysica Acta (BBA) - Enzymology. 391 (2): 326–33. doi:10.1016/0005-2744(75)90256-9. PMID 807246.
- ^ Sheikhnejad RG, Srivastava PN (June 1986). "Isolation and properties of a phosphatidylcholine-specific phospholipase C from bull seminal plasma". The Journal of Biological Chemistry. 261 (16): 7544–9. PMID 3086312.
- ^ Takahashi T, Sugahara T, Ohsaka A (May 1974). "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. doi:10.1016/0005-2795(74)90074-9. PMID 4365891.
External links
- Phospholipase+C at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
