Reference: Kilari RS, et al. (2013) Understanding inositol pyrophosphate metabolism and function: kinetic characterization of the DIPPs. FEBS Lett 587(21):3464-70

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Abstract


We illuminate the metabolism and the cell-signaling activities of inositol pyrophosphates, by showing that regulation of yeast cyclin-kinase by 1-InsP7 is not conserved for mammalian CDK5, and by kinetically characterizing Ddp1p/DIPP-mediated dephosphorylation of 1-InsP7, 5-InsP7 and InsP8. Each phosphatase exhibited similar Km values for every substrate (range: 35-148 nM). The rank order of kcat values (1-InsP7>5-InsP7=InsP8) was identical for each enzyme, although DIPP1 was 10- to 60-fold more active than DIPP2α/β and DIPP3α/β. We demonstrate InsP8 dephosphorylation preferentially progresses through 1-InsP7. Conversely, we conclude that the more metabolically and functionally significant steady-state route of InsP8 synthesis proceeds via 5-InsP7.

Reference Type
Journal Article | Research Support, N.I.H., Intramural | Research Support, Non-U.S. Gov't
Authors
Kilari RS, Weaver JD, Shears SB, Safrany ST
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