Enzyme

Download
EC Tree
     3. Hydrolases
        3.1 Acting on ester bonds
            3.1.4 Phosphoric-diester hydrolases
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:
PDBScop
2WY6 8026385; 8028716; 8038764; 8041095; 8026385; 8028716; 8038764; 8041095; 8026385; 8028716; 8038764; 8041095;
1QMD 8026385; 8028716; 8038764; 8041095; 8026385; 8028716; 8038764; 8041095;
1QM6 8026385; 8028716; 8038764; 8041095; 8026385; 8028716; 8038764; 8041095;
2WXU 8026385; 8028716; 8038764; 8041095;
2WXT 8026385; 8028716; 8038764; 8041095;
 » show all

Cath: 1.10.575.10; 3.60.10.10; 2.60.60.20;

3D structure

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.

References

External Links

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
MSA:

3.1.4.3;

Phylogenetic Tree:

3.1.4.3;

Uniprot:
M-CSA:
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

References

TitleAuthorsDatePubMed ID
Structure of the key toxin in gas gangrene.Naylor CE, Eaton JT, Howells A, Justin N, Moss DS, Titball RW, Basak AK1998 Aug9699639
Biochemical and molecular analysis of phospholipase C and phospholipase D activity in mycobacteria.Johansen KA, Gill RE, Vasil ML1996 Aug8757862
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 Z1989 Mar 232493587
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 J2013 Jan23089468
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 AK2002 May 3112051905
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 B1999 Dec 310610794