ID: | 3.1.4.3 |
---|---|
Description: | Phospholipase C. |
Alternative Name: |
Lipophosphodiesterase I. Lecithinase C. Clostridium welchii alpha-toxin. Clostridium oedematiens beta- and gamma-toxins. |
Prosite: | PDOC00357; |
PDB: |
» show all » hide |
Cath: | 1.10.575.10; 3.60.10.10; 2.60.60.20; |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.UniProtKB Enzyme Link: | UniProtKB 3.1.4.3 |
BRENDA Enzyme Link: | BRENDA 3.1.4.3 |
KEGG Enzyme Link: | KEGG3.1.4.3 |
BioCyc Enzyme Link: | BioCyc 3.1.4.3 |
ExPASy Enzyme Link: | ExPASy3.1.4.3 |
EC2PDB Enzyme Link: | EC2PDB 3.1.4.3 |
ExplorEnz Enzyme Link: | ExplorEnz 3.1.4.3 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.1.4.3 |
IntEnz Enzyme Link: | IntEnz 3.1.4.3 |
MEDLINE Enzyme Link: | MEDLINE 3.1.4.3 |
RHEA:10604 | a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-sn-glycerol + H(+) + phosphocholine |
RULE(radius=1) | [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[OH2;+0:7]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[OH;+0:7] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Structure of the key toxin in gas gangrene. | Naylor CE, Eaton JT, Howells A, Justin N, Moss DS, Titball RW, Basak AK | 1998 Aug | 9699639 |
Biochemical and molecular analysis of phospholipase C and phospholipase D activity in mycobacteria. | Johansen KA, Gill RE, Vasil ML | 1996 Aug | 8757862 |
High-resolution (1.5 A) crystal structure of phospholipase C from Bacillus cereus. | Hough E, Hansen LK, Birknes B, Jynge K, Hansen S, Hordvik A, Little C, Dodson E, Derewenda Z | 1989 Mar 23 | 2493587 |
The plant non-specific phospholipase C gene family. Novel competitors in lipid signalling. | Pokotylo I, Pejchar P, Potocký M, Kocourková D, Krčková Z, Ruelland E, Kravets V, Martinec J | 2013 Jan | 23089468 |
Crystal structure of the C. perfringens alpha-toxin with the active site closed by a flexible loop region. | Eaton JT, Naylor CE, Howells AM, Moss DS, Titball RW, Basak AK | 2002 May 31 | 12051905 |
Characterisation of the calcium-binding C-terminal domain of Clostridium perfringens alpha-toxin. | Naylor CE, Jepson M, Crane DT, Titball RW, Miller J, Basak AK, Bolgiano B | 1999 Dec 3 | 10610794 |