Glycerophosphoinositol inositolphosphodiesterase
| glycerophosphoinositol inositolphosphodiesterase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.4.43 | ||||||||
| CAS no. | 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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The enzyme glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43)[1][2][3][4] is an enzyme that catalyzes the chemical reaction
- 1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O glycerol + 1D-myo-inositol 1-phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric diester bonds. The systematic name 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.[5] Sekar and co-workers [6] clearly demonstrated the dissociation of 1-D-myo-inositol-1,2-cyclic-phosphate 2-inositolphosphohydrolase activity from annexin III. Perron and co-workers confirmed on the basis of structural studies that annexin III did not possess an enzymatic activity.[7] While the 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.[8]
References
- ^ Dawson RM, Hemington N (1977). "A phosphodiesterase in rat kidney cortex that hydrolyses glycerylphosphorylinositol". Biochem. J. 162 (2): 241–5. doi:10.1042/bj1620241. PMC 1164595. PMID 192216.
- ^ Dawson RM, Hemington N (1977). "A phosphodiesterase in rat kidney cortex that hydrolyses glycerylphosphorylinositol". Biochem. J. 162 (2): 241–5. doi:10.1042/bj1620241. PMC 1164595. PMID 192216.
- ^ 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): 59–67. doi:10.1042/bj1340059. 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): 851–6. doi:10.1016/S0021-9258(17)35251-1. PMID 1845995.
- ^ Ross, T S; Tait, J F; Majerus, P W (1990). "Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase with lipocortin III". Science. 248 (4955): 605–607. Bibcode:1990Sci...248..605R. doi:10.1126/science.2159184. PMID 2159184.
- ^ Sekar, M C; Sambandam, V; Grizzle, W E; McDonald, J M (1996). "Dissociation of cyclic inositol phosphohydrolase activity from annexin III". J. Biol. Chem. 271 (14): 8295–8299. doi:10.1074/jbc.271.14.8295. PMID 8626524.
- ^ Perron, B; LewitBentley, A; Geny, B; RussoMarie, F (1997). "Can enzymatic activity, or otherwise, be inferred from structural studies of annexin III?". J. Biol. Chem. 272 (17): 11321–11326. doi:10.1074/jbc.272.17.11321. PMID 9111038.
- ^ Sekar, M C; Scott, E D; Sambandam, V; Berry, R E (1997). "Demonstration of the presence of cyclic inositol phosphohydrolase in human urine". Biochem. Mol. Med. 62 (1): 95–100. doi:10.1006/bmme.1997.2629. PMID 9367804.
