PPIP5Ks (E.C. 188.8.131.52) are ATP-dependent, small molecule kinases that synthesize inositol pyrophosphates (PP-InsPs), which are intracellular signals with functionally significant and “energetic” phosphoanhydride bonds. The purification and cloning of these enzymes was first described in a body of work that was performed independently by two groups and published in 2007 (Choi et al. 2007; Fridy et al. 2007; Mulugu et al. 2007). PPIP5Ks are distributed throughout eukaryotic kingdoms; the orthologs have aliases: Asp1 in Schizosaccharomyces pombe, Vip1 in Saccharomyces cerevisiae, VIH in Arabidopsis thaliana. Since yeasts and plants diverged from the animal kingdom 1.3 and 1.5 billion years ago, respectively (see www.timetree.org), it is clear that PPIP5Ks are evolutionarily ancient enzymes. Two PPIP5K genes are expressed in both mammals and plants (Choi et al. 2007; Fridy et al. 2007; Laha et al. 2015; Mulugu et al. 2007).