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The effect of the myo-inositol 1,4,5-trisphosphate (IP3) analogue, myo-inositol 1,4,5-trisphosphorothioate (IPS3) on the dephosphorylation of D-5-[32P]IP3 by the 5-phosphatase from human erythrocyte membranes has been investigated. DL-IPS3 was found to act as a competitive inhibitor with a Ki of 6 microM, making it the most potent inhibitor currently available for this enzyme. L-IP3 inhibited the enzyme with a Ki of 124 microM and was more potent than D-2,3-diphosphoglycerate (Ki 978 microM).


Journal article


Febs lett

Publication Date





373 - 377


Erythrocytes, Humans, In Vitro Techniques, Inositol, Inositol 1,4,5-Trisphosphate, Inositol Polyphosphate 5-Phosphatases, Kinetics, Organothiophosphorus Compounds, Phosphoric Monoester Hydrolases