Activating Compound | Comment | Organism | Structure |
---|---|---|---|
butyl-fluorescein myo-inositol phosphate | two molecules bind to enzyme, one at the active site and one at a subsite, causing an increase in activity, kinetics | Bacillus cereus | |
dihexanoylphosphatidylcholine | non-substrate activator lipid, maximum PI-PLC activity at 0.7-1 mM | Bacillus cereus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of butyl-fluorescein myo-inositol phosphate and methyl-fluorescein myo-inositol phosphate cleavage, two-site kinetic model | Bacillus cereus | |
0.14 | - |
methyl-fluorescein myo-inositol phosphate | pH 7, 25°C, in presence of dihexanoylphosphatidylcholine | Bacillus cereus | |
0.81 | - |
methyl-fluorescein myo-inositol phosphate | pH 7, 25°C, in absence of dihexanoylphosphatidylcholine | Bacillus cereus |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
35000 | - |
1 * 35000 | Bacillus cereus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-phosphatidyl-1D-myo-inositol | Bacillus cereus | natural substrate | 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus cereus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol | mechanism | Bacillus cereus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
1-phosphatidyl-1D-myo-inositol | natural substrate | Bacillus cereus | 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol | - |
? | |
1-phosphatidyl-1D-myo-inositol | cleaves phosphatidylinositol in a rapid intramolecular transphosphorylation reaction forming the products, in a second reaction the cyclic phosphorylase activity of PI-PLC catalyzes the slow hydrolysis of 1D-myo-inositol 1,2-cyclic phosphate to D-myo-inositol 1-phosphate, utilizes His-32 and His-82 in a general acid catalysis mechanism | Bacillus cereus | 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol | - |
? | |
butyl-fluorescein myo-inositol phosphate | two substrate molecules bind to enzyme, one at the active site and one at a subsite, causing an increase in activity, subsite interactions of PI-PLC | Bacillus cereus | D-myo-inositol 1,2-cyclic phosphate + butyl-fluorescein | - |
? | |
methyl-fluorescein myo-inositol phosphate | substrate binds only to the active site and not to the activator site | Bacillus cereus | D-myo-inositol 1,2-cyclic phosphate + methyl-fluorescein | - |
? |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 35000 | Bacillus cereus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Bacillus cereus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Bacillus cereus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Bacillus cereus |