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• W2090430216 abstract "Ins(1,4,5,6)P 4 , a biologically active cell constituent, was recently advocated as a substrate of human Ins(3,4,5,6)P 4 1‐kinase (hITPK1), because stereochemical factors were believed relatively unimportant to specificity [Miller, G.J., Wilson, M.P., Majerus, P.W. and Hurley, J.H. (2005) Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4‐triphosphate 5/6‐kinase. Mol. Cell. 18, 201–212]. Contrarily, we provide three examples of hITPK1 stereospecificity. hITPK1 phosphorylates only the 1‐hydroxyl of both Ins(3,5,6)P 3 and the meso‐ compound, Ins(4,5,6)P 3 . Moreover, hITPK1 has >13,000‐fold preference for Ins(3,4,5,6)P 4 over its enantiomer, Ins(1,4,5,6)P 4 . The biological significance of hITPK1 being stereospecific, and not physiologically phosphorylating Ins(1,4,5,6)P 4 , is reinforced by our demonstrating that Ins(1,4,5,6)P 4 is phosphorylated ( K m = 0.18 μM) by inositolphosphate‐multikinase." @default.
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• W2090430216 date "2005-12-19" @default.
• W2090430216 modified "2023-10-17" @default.
• W2090430216 title "On the contribution of stereochemistry to human ITPK1 specificity: Ins(1,4,5,6)P₄is not a physiologic substrate" @default.
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• W2090430216 doi "https://doi.org/10.1016/j.febslet.2005.12.016" @default.
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