The purification and properties of myo-inositol monophosphatase from bovine brain

N. S. Gee*, C. I. Ragan, K. J. Watling, S. Aspley, R. G. Jackson, G. G. Reid, D. Gani, J. K. Shute

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


1. An inositol monophosphatase was purified to homogeneity from bovine brain. 2. The enzyme is a dimer of subunit Mr 29,000. 3. The enzyme hydrolyses both enantiomers of myo-inositol 1-phosphate and both enantiomers of myo-inositol 4-phosphate, but has no activity towards inositol bisphosphates, inositol trisphosphates or inositol 1,3,4,5-tetrakisphosphate. 4. Several non-inositol-containing monophosphates are also substrates. 5. The enzyme requires Mg2+ for activity, and Zn2+ supports activity to a small extent. 6. Other bivalent cations (including Zn2+) are inhibitors, competitive with Mg2+. 7. Phosphate, but not inositol, is an inhibitor competitive with substrate. 8. Li+ inhibits hydrolysis of inositol 1-phosphate and inositol 4-phosphate uncompetitively with different apparent Ki values (1.0 mM and 0.26 mM respectively).

Original languageEnglish
Pages (from-to)883-889
Number of pages7
JournalThe Biochemical journal
Issue number3
Publication statusPublished - 1 Feb 1988


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