Inositol pyrophosphates (diphosphoinositol phosphates) are reported agents of phosphate homeostasis, disease resistance, and hormone action in plants. Of the enzymes that have been shown to synthesize inositol pyrophosphates, inositol tris/tetrakisphosphate (ITPK)1 and Arabidopsis thaliana diphosphoinositol pentakisphosphate kinase (VIH)1/VIH2 share the ATP-grasp fold—the latter also possesses a phosphatase domain. Among ATP-grasp inositol phosphate kinases, ITPK1 is particularly flexible—phosphorylating equatorial hydroxyls and equatorial phosphates on inositol phosphates. Herein, we show that the combination of ITPK1 and inositol pentakisphosphate 2-kinase (IPK1) is sufficient to synthesize 5-PP-InsP5 from 1D-myo-inositol 3-monophosphate (Ins3P) and that ITPK1 is capable of converting 1D-myo-inositol 1-monophosphate to myo-inositol 1,3,4,5,6-pentakisphosphate [Ins(1,3,4,5,6)P5]. In defining a minimal catalytic unit for synthesis of both myo-inositol 1,2,3,4,5,6-hexakisphosphate (InsP6/Ins(1,2,3,4,5,6)P6) and 5-PP-InsP5, we define the minimum enzymology of the ‘lipid-independent’ pathway of InsP6 synthesis from Ins3P and its intermediates. The pathway proceeds: Ins3P, 1D-myo-inositol 3,4-bisphosphate, 1D-myo-inositol 3,4,5-trisphosphate, 1D-myo-inositol 3,4,5,6-tetrakisphosphate, Ins(1,3,4,5,6)P5, Ins(1,2,3,4,5,6)P6, and therefrom to 5-diphosphoinositol-1,2,3,4,6-pentakisphosphate [5-PP-Ins(1,2,3,4,6)P5].
A minimum catalytic unit for synthesis of InsP6 and 5-PP-InsP5 in Arabidopsis
H. Whitfield,Colleen Sprigg,Andrew M. Riley,Barry V L Potter,Hui-Fen Kuo,Charles A. Brearley
Published 2025 in Biochemical Journal
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- Publication year
2025
- Venue
Biochemical Journal
- Publication date
2025-11-10
- Fields of study
Biology, Medicine, Chemistry, Environmental Science
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Semantic Scholar, PubMed
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