EC number:4.6.1.13
Enzyme
Download| EC Tree |
| 4. Lyases |
| 4.6 Phosphorus-oxygen lyases |
| 4.6.1 Phosphorus-oxygen lyases (only sub-subclass identified to date) |
| ID: | 4.6.1.13 |
|---|---|
| Description: | Phosphatidylinositol diacylglycerol-lyase. |
| Alternative Name: |
Phosphatidylinositol phospholipase C. Monophosphatidylinositol phosphodiesterase. 1-phosphatidylinositol phosphodiesterase. |
| Cath: | 1.10.238.10; 1.20.1230.10; 3.20.20.190; 3.30.505.10; 2.30.29.240; 2.30.29.30; 2.30.30.40; 2.60.40.150; 3.10.20.90; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 4.6.1.13 |
| BRENDA Enzyme Link: | BRENDA 4.6.1.13 |
| KEGG Enzyme Link: | KEGG4.6.1.13 |
| BioCyc Enzyme Link: | BioCyc 4.6.1.13 |
| ExPASy Enzyme Link: | ExPASy4.6.1.13 |
| EC2PDB Enzyme Link: | EC2PDB 4.6.1.13 |
| ExplorEnz Enzyme Link: | ExplorEnz 4.6.1.13 |
| PRIAM enzyme-specific profiles Link: | PRIAM 4.6.1.13 |
| IntEnz Enzyme Link: | IntEnz 4.6.1.13 |
| MEDLINE Enzyme Link: | MEDLINE 4.6.1.13 |
| RHEA:17093 | a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) = 1D-myo-inositol 1,2-cyclic phosphate + a 1,2-diacyl-sn-glycerol |
| RULE(radius=1) | ([*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[*:7]-[OH;+0:8])>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[O;H0;+0:8]-[*:7] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| The catalytic role of aspartate in a short strong hydrogen bond of the Asp274-His32 catalytic dyad in phosphatidylinositol-specific phospholipase C can be substituted by a chloride ion. | Zhao L, Liao H, Tsai MD | 2004 Jul 30 | 15155721 |
| Investigating the interfacial binding of bacterial phosphatidylinositol-specific phospholipase C. | Wehbi H, Feng J, Kolbeck J, Ananthanarayanan B, Cho W, Roberts MF | 2003 Aug 12 | 12899624 |
| Allosteric interactions within subsites of a monomeric enzyme: kinetics of fluorogenic substrates of PI-specific phospholipase C. | Birrell GB, Zaikova TO, Rukavishnikov AV, Keana JF, Griffith OH | 2003 May | 12719256 |
| Engineering a catalytic metal binding site into a calcium-independent phosphatidylinositol-specific phospholipase C leads to enhanced stereoselectivity. | Kravchuk AV, Zhao L, Bruzik KS, Tsai MD | 2003 Mar 4 | 12600209 |
| A catalytic diad involved in substrate-assisted catalysis: NMR study of hydrogen bonding and dynamics at the active site of phosphatidylinositol-specific phospholipase C. | Ryan M, Liu T, Dahlquist FW, Griffith OH | 2001 Aug 14 | 11583175 |
| Mechanism of phosphatidylinositol-specific phospholipase C: origin of unusually high nonbridging thio effects. | Kravchuk AV, Zhao L, Kubiak RJ, Bruzik KS, Tsai MD | 2001 May 8 | 11331007 |