Cloned (Comment) | Organism |
---|---|
- |
Bacillus cereus |
Crystallization (Comment) | Organism |
---|---|
X-ray crystal structure | Bacillus cereus |
Protein Variants | Comment | Organism |
---|---|---|
D274A | mutation of an catalytic diad residue, mutant with abolished activity, NMR study | Bacillus cereus |
D274N | mutation of an catalytic diad residue, 4.2% of wild-type activity | Bacillus cereus |
H32A | mutation of an catalytic diad residue, mutant with abolished activity, NMR study | Bacillus cereus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus cereus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant PI-PLC | 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 | a catalytic diad at the active site composed of Asp-274 and His-32 is involved in substrate-assisted catalysis, its function is to hydrogen-bond with the 2-OH of phosphatidylinositol to form a catalytic triad, catalytic mechanism | Bacillus cereus | 1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol | PI-PLC catalyzes in a second step the slow hydrolysis of 1D-myo-inositol 1,2-cyclic phosphate to form myo-inositol 1-phosphate | ? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Bacillus cereus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7 | - |
assay at | Bacillus cereus |