EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
4.6.1.13 | 1-phosphatidyl-1D-myo-inositol |
- |
Bacillus cereus |
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol |
- |
? |
4.6.1.13 | 1-phosphatidyl-1D-myo-inositol |
natural substrate |
Bacillus cereus |
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol |
- |
? |
4.6.1.13 | 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 |
? |
4.6.1.13 | 1-phosphatidyl-1D-myo-inositol |
aggregated substrate is preferred over monomeric substrate |
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 | 1-phosphatidyl-1D-myo-inositol |
catalytic mechanism, role of Arg-69, the bidentate nature of Arg-69 is the origin of the large thio effects and stereoselectivity in PI-PLC, its function is to bring the phosphate group and the 2-OH group of inositol into proximity and to induce proper alignment for nucleophilic attack, and possibly to lower the pKa of the 2-OH |
Bacillus sp. (in: Bacteria) |
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol |
- |
? |
4.6.1.13 | 1-phosphatidyl-1D-myo-inositol |
catalyzes the cleavage of the phosphorus-oxygen bond in phosphatidylinositol, catalytic role of aspartate in a short strong hydrogen bond of the Asp274-His32 catalytic dyad, catalytic mechanism, active site structure |
Bacillus thuringiensis |
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol |
- |
? |
4.6.1.13 | 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 |
- |
? |
4.6.1.13 | 1-phosphatidyl-1D-myo-inositol |
general acid/general base mechanism, enhanced activity when phosphatidylinositol is present in an interface compared to monomeric substrate |
Bacillus thuringiensis |
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol |
PI-PLC catalyzes the hydrolysis of myo-inositol 1,2-cyclic phosphate to myo-inositol 1-phosphate |
? |
4.6.1.13 | 1-phosphatidyl-1D-myo-inositol |
PLC accepts only nonphosphorylated phosphatidylinositol substrates and produces cyclic inositol phosphate as final product, which is hydrolyzed at a 1000fold lower rate, catalytic mechanism, uses a guanidinium group of Arg-69 during catalysis |
Bacillus sp. (in: Bacteria) |
1D-myo-inositol 1,2-cyclic phosphate + diacylglycerol |
- |
? |
4.6.1.13 | 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 |
- |
? |