| EC |
3.1.4.3 |
| Accepted name: |
phospholipase C |
| Reaction: |
a phosphatidylcholine + H2O = 1,2-diacyl-sn-glycerol + phosphocholine |
| Other name(s): |
lipophosphodiesterase I; lecithinase C; Clostridium welchii α-toxin; Clostridium oedematiens β- and γ-toxins; lipophosphodiesterase C; phosphatidase C; heat-labile hemolysin; α-toxin |
| Systematic name: |
phosphatidylcholine cholinephosphohydrolase |
| Comments: |
The bacterial enzyme, which is a zinc protein, also acts on sphingomyelin and phosphatidylinositol; that from seminal plasma does not act on phosphatidylinositol. |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9001-86-9 |
| References: |
| 1. |
Druzhinina, K.V. and Kritzman, M.G. [Lecithinase from animal tissues.] Biokhimiya 17 (1952) 77–81. [PMID: 13066482] (in Russian) |
| 2. |
Little, C. and Otnass, A.-B. The metal ion dependence of phospholipase C from Bacillus cereus. Biochim. Biophys. Acta 391 (1975) 326–333. [DOI] [PMID: 807246] |
| 3. |
Sheiknejad, R.G. and Srivastava, P.N. Isolation and properties of a phosphatidylcholine-specific phospholipase C from bull seminal plasma. J. Biol. Chem. 261 (1986) 7544–7549. [PMID: 3086312] |
| 4. |
Takahashi, T., Sugahara, T. and Ohsaka, A. Purification of Clostridium perfringens phospholipase C (α-toxin) by affinity chromatography on agarose-linked egg-yolk lipoprotein. Biochim. Biophys. Acta 351 (1974) 155–171. [DOI] [PMID: 4365891] |
|
| [EC 3.1.4.3 created 1961] |
| |
|
| |
|
Printable version