Lecithinase C
Phospholipase C | |||||||||
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Identifiers | |||||||||
EC number | 3.1.4.3 | ||||||||
CAS number | 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 | ||||||||
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Phospholipase C (EC 3.1.4.3, lipophosphodiesterase I, Clostridium welchii alpha-toxin, Clostridium oedematiens beta- and gamma-toxins, lipophosphodiesterase C, phosphatidase C, heat-labile hemolysin, alpha-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, K.V.; Kritzman, M.G. (1952). "[Lecithinase from animal tissues.]". Biokhimiya. 17: 77–81. PMID 13066482.
- ↑ Little, C.; Otnass, A.-B. (1975). "The metal ion dependence of phospholipase C from Bacillus cereus". Biochim. Biophys. Acta. 391: 326–333. doi:10.1016/0005-2744(75)90256-9. PMID 807246.
- ↑ Sheiknejad, R.G.; Srivastava, P.N. (1986). "Isolation and properties of a phosphatidylcholine-specific phospholipase C from bull seminal plasma". J. Biol. Chem. 261: 7544–7549. PMID 3086312.
- ↑ Takahashi, T.; Sugahara, T.; Ohsaka, A. (1974). "Purification of Clostridium perfringens phospholipase C (α-toxin) by affinity chromatography on agarose-linked egg-yolk lipoprotein". Biochim. Biophys. Acta. 351: 155–171. doi:10.1016/0005-2795(74)90074-9. PMID 4365891.
External links
- Phospholipase C at the US National Library of Medicine Medical Subject Headings (MeSH)
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