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Glycerophosphoinositol inositolphosphodiesterase

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glycerophosphoinositol inositolphosphodiesterase
Identifiers
EC no.3.1.4.43
CAS no.9076-91-9
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The enzyme glycerophosphoinositol inositolphosphodiesterase (EC 3.1.4.43) is an enzyme that catalyzes the chemical reaction

1-(sn-glycero-3-phospho)-1D-myo-inositol + H2O {\displaystyle \rightleftharpoons } 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. Sekar and co-workers 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. While the 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.

References

  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.
Hydrolase: esterases (EC 3.1)
3.1.1: Carboxylic
ester hydrolases
3.1.2: Thioesterase
3.1.3: Phosphatase
3.1.4:
Phosphodiesterase
3.1.6: Sulfatase
Nuclease (includes
deoxyribonuclease
and ribonuclease)
3.1.11-16:
Exonuclease
Exodeoxyribonuclease
Exoribonuclease
3.1.21-31:
Endonuclease
Endodeoxyribonuclease
Endoribonuclease
either deoxy- or ribo-    
Enzymes
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Regulation
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