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Literature summary extracted from
- Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C (2002), J. Biol. Chem., 277, 19867-19875.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.6.1.13 | Isopropanol | 30%, activates | Bacillus thuringiensis |  |
| 4.6.1.13 | additional information | PI-PLC exhibits several types of kinetic interfacial activation by interfaces, roles of Trp-47 and Trp-242 | Bacillus thuringiensis | |
| 4.6.1.13 | phosphatidylcholine | activates | Bacillus thuringiensis | |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 4.6.1.13 | overexpression in Escherichia coli BL21 | Bacillus thuringiensis |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 4.6.1.13 | W178A | mutant with reduced stability and specific activity, study of kinetic activation by micellar phosphatidylcholine | Bacillus thuringiensis |
| 4.6.1.13 | W242A | active enzyme, partitioning of mutant enzyme to vesicles is decreased by more than 10fold, study of kinetic activation by micellar phosphatidylcholine | Bacillus thuringiensis |
| 4.6.1.13 | W242F | kinetic analysis, binding studies to phosphatidylcholine vesicles | Bacillus thuringiensis |
| 4.6.1.13 | W242I | kinetic analysis, binding studies to phosphatidylcholine vesicles | Bacillus thuringiensis |
| 4.6.1.13 | W280A | mutant with reduced stability, study of kinetic activation by micellar phosphatidylcholine | Bacillus thuringiensis |
| 4.6.1.13 | W47A | active enzyme, partitioning of mutant enzyme to vesicles is decreased by more than 10fold, study of kinetic activation by micellar phosphatidylcholine | Bacillus thuringiensis |
| 4.6.1.13 | W47A/W242A | double mutant, no affinity for phospholipid surfaces, no kinetic activation by micellar phosphatidylcholine | Bacillus thuringiensis |
| 4.6.1.13 | W47F | kinetic analysis, binding studies to phosphatidylcholine vesicles | Bacillus thuringiensis |
| 4.6.1.13 | W47I | kinetic analysis, binding studies to phosphatidylcholine vesicles | Bacillus thuringiensis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 4.6.1.13 | myo-inositol | poor competitive inhibitor | Bacillus thuringiensis | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 4.6.1.13 | additional information | - |
additional information | kinetic data | Bacillus thuringiensis |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 4.6.1.13 | cytoplasm | recombinant PI-PLC, expressed in Escherichia coli BL21 | Bacillus thuringiensis | 5737 | - |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 4.6.1.13 | Bacillus thuringiensis | - |
- |
- |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 4.6.1.13 | additional information | - |
specific activities of wild-type and mutant PI-PLCs towards 1D-myo-inositol 1,2-cyclic phosphate in the absence and presence of different activators | Bacillus thuringiensis |
| 4.6.1.13 | 401 | - |
W47I mutant PI-PLC, phosphotransferase activity | Bacillus thuringiensis |
| 4.6.1.13 | 556 | - |
wild-type PI-PLC, phosphotransferase activity | Bacillus thuringiensis |
| 4.6.1.13 | 558 | - |
W47F mutant PI-PLC, phosphotransferase activity | Bacillus thuringiensis |
| 4.6.1.13 | 658 | - |
W242F mutant PI-PLC, phosphotransferase activity | Bacillus thuringiensis |
| 4.6.1.13 | 684 | - |
W242I mutant PI-PLC, phosphotransferase activity | Bacillus thuringiensis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 4.6.1.13 | 1-phosphatidyl-1D-myo-inositol | Trp-47 and Trp-242 residues are important for enzyme to bind to interfaces, both activating zwitterionic and substrate anionic surfaces, micellar phosphatidylinositol is a better substrate than monomeric phosphatidylinositol | Bacillus thuringiensis | 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol | a cyclic phosphodiesterase activity of PI-PLC converts 1D-myo-inositol 1,2-cyclic phosphate to inositol 1-phosphate | ? | |
| 4.6.1.13 | additional information | not: phosphatidylcholine | Bacillus thuringiensis | ? | - |
? | |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 4.6.1.13 | 41.5 | - |
Tm-value, pH 8, W178A mutant PI-PLC | Bacillus thuringiensis |
| 4.6.1.13 | 47 | - |
Tm-value, pH 8, W280A mutant PI-PLC | Bacillus thuringiensis |
| 4.6.1.13 | 53.6 | - |
Tm-value, pH 8, W47A mutant PI-PLC | Bacillus thuringiensis |
| 4.6.1.13 | 54.4 | - |
Tm-value, pH 8, wild-type PI-PLC | Bacillus thuringiensis |
| 4.6.1.13 | 54.6 | - |
Tm-value, pH 8, W47A/W242A double mutant PI-PLC | Bacillus thuringiensis |
| 4.6.1.13 | 56.2 | - |
Tm-value, pH 8, W242A mutant PI-PLC | Bacillus thuringiensis |
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