2.7.4.24: diphosphoinositol-pentakisphosphate 1-kinase
This is an abbreviated version!
For detailed information about diphosphoinositol-pentakisphosphate 1-kinase, go to the full flat file.
Word Map on EC 2.7.4.24
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2.7.4.24
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pyrophosphate
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polyphosphate
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pp-insps
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hexakisphosphate
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5-insp7
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tetrakisphosphate
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bisdiphosphoinositol
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spx
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medicine
- 2.7.4.24
- pyrophosphate
- polyphosphate
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pp-insps
- hexakisphosphate
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5-insp7
- tetrakisphosphate
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bisdiphosphoinositol
- spx
- medicine
Reaction
Synonyms
ATP:5-diphospho-1D-myo-inositol-pentakisphosphate phosphotransferase, diphospho-myo-inositol pentakisphosphate 5-kinase, diphosphoinositol pentakisphosphate kinase, diphosphoinositol pentakisphosphate kinase 2, diphosphoinositol-pentakisphosphate 1/3-kinase, diphosphoinositol-pentakisphosphate kinase, EC 2.7.1.155, IP7 kinase, kinase (phosphorylating), diphosphoinositol 1,2,3,4,5-pentakisphosphate 5-, More, PP-InsP5 kinase, PP-IP5 kinase, PPIP5K, PPIP5K1, PPIP5K2, VIP, VIP1, VIP2
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General Information
General Information on EC 2.7.4.24 - diphosphoinositol-pentakisphosphate 1-kinase
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evolution
physiological function
additional information
a time-resolved, fluorescence resonance energy transfer ADP-assay is optimized. Inhibition is competitive with ATP
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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
evolution
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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
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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
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
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
physiological function
mice homozygous for a targeted deletion of the Ppip5k2 phosphatase domain exhibit degeneration of cochlear outer hair cells and elevated hearing thresholds
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