Arabidopsis ITPK1 and ITPK2 have an Evolutionary Conserved Phytic Acid Kinase Activity.

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ID: 51451
2019
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Abstract
Diphospho-myo-inositol polyphosphates, also termed inositol pyrophosphates, are molecular messengers containing at least one high-energy phosphoanhydride bond and regulate a wide range of cellular processes in eukaryotes. While inositol pyrophosphates InsP and InsP are present in different plant species, both the identity of enzymes responsible for InsP synthesis and the isomer identity of plant InsP remain unknown. This study demonstrates that Arabidopsis ITPK1 and ITPK2 catalyze the phosphorylation of phytic acid (InsP) to the symmetric InsP isomer 5-InsP and that InsP kinase activity of ITPK enzymes is evolutionarily conserved from humans to plants. We also show by P NMR that plant InsP is structurally identical to the in vitro InsP kinase products of ITPK1 and ITPK2. Our findings lay the biochemical and genetic basis to uncover physiological processes regulated by 5-InsP in plants.
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laha2019arabidopsisacs Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Laha, Debabrata;Parvin, Nargis;Hofer, Alexandre;Giehl, Ricardo F H;Fernandez-Rebollo, Nicolas;von Wiren, Nicolaus;Saiardi, Adolfo;Jessen, Henning J;Schaaf, Gabriel;
Journal ACS chemical biology
Year 2019
DOI
10.1021/acschembio.9b00423
URL
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