Glycerophosphoinositol inositolphosphodiesterase explained

glycerophosphoinositol inositolphosphodiesterase
Ec Number:3.1.4.43
Cas Number:9076-91-9
Go Code:0047394

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

\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.[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]

Notes and References

  1. Dawson RM, Hemington N . 1977 . A phosphodiesterase in rat kidney cortex that hydrolyses glycerylphosphorylinositol . Biochem. J. . 162 . 241 - 5 . 192216 . 2 . 10.1042/bj1620241 . 1164595.
  2. Dawson RM, Hemington N . 1977 . A phosphodiesterase in rat kidney cortex that hydrolyses glycerylphosphorylinositol . Biochem. J. . 162 . 241 - 5 . 192216 . 2 . 10.1042/bj1620241 . 1164595 .
  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 . 59 - 67 . 4353088 . 1 . 10.1042/bj1340059 . 1177787 .
  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 . 851 - 6 . 1845995 . 2 . 10.1016/S0021-9258(17)35251-1 . free .
  5. 10.1126/science.2159184. Ross . T S. Tait . J F . Majerus . P W. Science. 248. 605–607. 1990. Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase with lipocortin III. 4955 . 2159184 . 1990Sci...248..605R .
  6. 10.1074/jbc.271.14.8295. Sekar . M C. Sambandam . V. Grizzle . W E. McDonald . J M. Dissociation of cyclic inositol phosphohydrolase activity from annexin III. J. Biol. Chem.. 271. 14. 8295–8299. 1996. 8626524 . free .
  7. Can enzymatic activity, or otherwise, be inferred from structural studies of annexin III?. Perron . B. LewitBentley . A. Geny . B. RussoMarie . F. J. Biol. Chem.. 272 . 17. 11321–11326. 1997. 10.1074/jbc.272.17.11321 . 9111038 . free .
  8. 10.1006/bmme.1997.2629 . Demonstration of the presence of cyclic inositol phosphohydrolase in human urine. Sekar . M C. Sambandam . V. Scott . E D. Berry . R E. Biochem. Mol. Med.. 62 . 1. 95–100. 1997. 9367804.

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