Glycerophosphoinositol inositolphosphodiesterase
| glycerophosphoinositol inositolphosphodiesterase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.1.4.43 | ||||||||
| CAS number | 9076-91-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) is an enzyme that catalyzes the chemical reaction
- 1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O glycerol + 1D-myo-inositol 1-phosphate
Thus, the two substrates of this enzyme are 1-(sn-glycero-3-phospho)-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-(sn-glycero-3-phospho)-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 [Ross et al., Science, 248: 605-607, 1990]. Sekar et al. [J Biol. Chem. 271: 8295-8299, 1996] clearly demonstrated the dissociation of 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase activity from annexin III. Perron et al. [J. Biol. Chem. 272:11321-11326, 1997] 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. [Biochem. Mol. Med. 61:95-100, 1007] reported over 10-fold increased release of this enzymatic activity in several patients admitted to the hospital's intensive care unit.
References
- Dawson RM, Hemington N (1977). "A phosphodiesterase in rat kidney cortex that hydrolyses glycerylphosphorylinositol". Biochem. J. 162 (2): 241&ndash, 5. PMC 1164595. PMID 192216.
- Dawson RM, Clarke N (1972). "D-myoinositol 1:2-cyclic phosphate 2-phosphohydrolase". Biochem. J. 127 (1): 113&ndash, 8. PMC 1178565. PMID 4342209.
- Dawson RM, Clarke NG (1973). "A comparison of D-inositol 1:2-cyclic phosphate 2-phosphohydrolase with other phosphodiesterases of kidney". Biochem. J. 134 (1): 59&ndash, 67. PMC 1177787. PMID 4353088.
- Ross TS, Majerus PW (1991). "Inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase. Substrate specificity and regulation of activity by phospholipids, metal ion chelators, and inositol 2-phosphate". J. Biol. Chem. 266 (2): 851&ndash, 6. PMID 1845995.