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Literature summary for 4.6.1.13 extracted from
- Optimizing the interfacial binding and activity of a bacterial phosphatidylinositol-specific phospholipase C (2003), J. Biol. Chem., 278, 24651-24657.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| diheptanoyl phosphatidylcholine | activates | Bacillus thuringiensis |  |
| Isopropanol | water-miscible, 30%, activates | Bacillus thuringiensis | |
| phosphatidylcholine | PI-PLC is activated by nonsubstrate interfaces such as phosphatidylcholine micelles or bilayers, activation corresponds with partial insertion into the interface of Trp-47 and Trp-242 in the rim of the alphabeta-barrel | Bacillus thuringiensis | |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| overexpression in Escherichia coli BL21 | Bacillus thuringiensis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| G238W | study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol | Bacillus thuringiensis |
| G238W/W242A | double mutant with enhanced activation and affinity for phosphatidylcholine interfaces above that of wild-type PI-PLC | Bacillus thuringiensis |
| G48W/W47A | double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol | Bacillus thuringiensis |
| I43W/W47A | double mutant with recovered kinetic interfacial activation, lower specific activity than wild-type PI-PLC | Bacillus thuringiensis |
| M49W/W47A | double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol | Bacillus thuringiensis |
| additional information | tryptophan rescue mutagenesis, reinsertion of a Trp at a different place in helix B in the W47A mutant or in the loop of the W242A mutant | Bacillus thuringiensis |
| N243W/W242A | double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol | Bacillus thuringiensis |
| Q45W/W47A | double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol | Bacillus thuringiensis |
| S236W/W242A | double mutant, study of the kinetic activation by diheptanoyl phosphatidylcholine and water-miscible isopropanol | Bacillus thuringiensis |
| W242A | mutant with much weaker binding to interfaces and lower kinetic interfacial activation | Bacillus thuringiensis |
| W47A | mutant with much weaker binding to interfaces and lower kinetic interfacial activation | Bacillus thuringiensis |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| isopropanol | water-miscible, 30%, activates | Bacillus thuringiensis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus thuringiensis | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant PI-PLC | Bacillus thuringiensis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Bacillus thuringiensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 1-phosphatidyl-1D-myo-inositol | the active site is located at the C-terminal side | Bacillus thuringiensis | 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol | - |
? | |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 54.4 | - |
Tm-value, wild-type PI-PLC | Bacillus thuringiensis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7 | - |
assay at | Bacillus thuringiensis |
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