Abstract
The Role of Phosphatases in Inositol Signaling Reactions
Highlights
The first 5-phosphatase enzymes studied were those that hydrolyze inositol 1,4,5-trisphosphate (Ins-1,4,5-P3)1 to inositol 1,4-bisphosphate (Ins-1,4-P2) [1,2,3]
There are eight distinct mammalian enzymes that are products of different genes for which cDNA clones have been isolated (Fig. 1). Several of these cDNAs exist in alternatively spliced versions, the significance of which is for the most part unknown. 5-Phosphatases are found in plants, Caenorhabditis elegans, and Drosophila, and there are four yeast genes that encode 5-phosphatase
The platelet type I enzyme is a representative of this group, which includes members cloned from dog thyroid and placenta [9, 10]
Summary
The first 5-phosphatase enzymes studied were those that hydrolyze inositol 1,4,5-trisphosphate (Ins-1,4,5-P3)1 to inositol 1,4-bisphosphate (Ins-1,4-P2) [1,2,3]. These enzymes are designated as inositol polyphosphate 5-phosphatases as the known substrates have multiple phosphate groups. They are the most active against these substrates of all 5-phosphatases and probably function as the enzymes that terminate calcium signaling. Group II enzymes hydrolyze all four 5-phosphatase substrates with varying catalytic efficiency.
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