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. 1988 Feb 1;249(3):883–889. doi: 10.1042/bj2490883

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

N S Gee 1, C I Ragan 1, K J Watling 1, S Aspley 1, R G Jackson 1, G G Reid 1, D Gani 1, J K Shute 1
PMCID: PMC1148789  PMID: 2833231

Abstract

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).

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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