Glycerophosphoinositol inositolphosphodiesterase


In enzymology, a glycerophosphoinositol inositolphosphodiesterase is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are 1--1D-myo-inositol and H2O, whereas its two products are glycerol and 1D-myo-inositol 1-phosphate.
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name of this enzyme class is 1--1D-myo-inositol inositolphosphohydrolase. Other names in common use include 1,2-cyclic-inositol-phosphate phosphodiesterase, D-myo-inositol 1:2-cyclic phosphate 2-phosphohydrolase, D-inositol 1,2-cyclic phosphate 2-phosphohydrolase, D-myo-inositol 1,2-cyclic phosphate 2-phosphohydrolase, 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase, and inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase.
This enzyme 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase, was reported to be identical to annexin III . Sekar et al. clearly demonstrated the dissociation of 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase activity from annexin III. Perron et al. confirmed based on structural studies that annexin III did not possess an enzymatic activity. While physiological significance of this enzymatic activity is still not clear, Sekar et al. reported over 10-fold increased release of this enzymatic activity in several patients admitted to the hospital's intensive care unit.