EC Number |
General Information |
Reference |
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2.7.4.24 | evolution |
positional specificity of the mammalian and yeast VIP/diphosphoinositol pentakisphosphate kinase family of inositol phosphate kinases, overview. The mammalian and yeast VIP/PPIP5K family enzymes phosphorylate the 1/3-position of the inositol ring in vitro and in vivo, phylogenetic variability within the crown taxa in the structures of inositol pyrophosphates, overview |
717780 |
2.7.4.24 | more |
a time-resolved, fluorescence resonance energy transfer ADP-assay is optimized. Inhibition is competitive with ATP |
762215 |
2.7.4.24 | physiological function |
1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate kinase activity is dominant when PPIP5K1 is expressed in intact cells. 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate phosphatase activity prevails when the enzyme is isolated from its cellular environment. Exogenous expression of PPIP5K1 in Drosophila melanogaster S3 cells elevates levels of 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate and 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate |
760744 |
2.7.4.24 | physiological function |
levels of both 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate and ATP decrease upon phosphate starvation and subsequently recover during phosphate replenishment |
761474 |
2.7.4.24 | physiological function |
mice homozygous for a targeted deletion of the Ppip5k2 phosphatase domain exhibit degeneration of cochlear outer hair cells and elevated hearing thresholds |
762199 |
2.7.4.24 | physiological function |
the enzyme synthesizes high-energy inositol pyrophosphates, which regulate cell function at the interface between cellular energy metabolism and signal transduction. Inhibition is competitive with ATP |
762215 |
2.7.4.24 | physiological function |
the yeast VIP/PPIP5K family enzymes phosphorylate the 1/3-position of the inositol ring in vitro and in vivo, and convert inositol hexakisphosphate to 1/3-diphosphoinositol pentakisphosphate with determination of unequivocally 1/3,5-(PP)2-IP4 is the isomeric structure of the bis-diphosphoinositol tetrakisphosphate |
717780 |