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evolution
differential spatial and temporal expression profiling of gene GmIpk1 and its two homologues Glyma06g03310 and Glyma04g03310 in Glycine max
evolution
most residues involved in substrate binding and catalysis are conserved between mammal and plant IP5 2-Ks, but some differences in the inositide P1 and P3 coordination are observed. InmIP5 2-K, additional interactions with P1 are produced through the side chain of Lys173, a residue non-conserved with the plant IP5 2-Ks but absolutely conserved in mammal enzymes, whereas conservative substitutions can be observed in other vertebrates
evolution
the amino acid sequence of GmIPK1 shows much similarity with that of Phaseolus vulgaris and Cicer arietinum. It also shows the presence of the characteristic Ins_P5_2-kinase domain required for catalytic activity
malfunction
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a functional Asp1 kinase domain abolishes invasive growth which is monopolar
malfunction
a loss-of-function mutant exhibits disturbed phosphate homeostasis and overaccumulated phosphate as a consequence of increased phosphate uptake activity and root-to-shoot phosphate translocation. The mutant also shows a phosphate deficiency-like root system architecture with reduced primary root and enhanced lateral root growth
malfunction
a mutant of inositol pentakisphosphate 2-kinase displays hypersensitivity to arsenate stress and less arsenate uptake when compared to the wild type enzyme
malfunction
cells lacking the enzyme display defects in dynein-dependent trafficking pathways including endosomal sorting, vesicle movement and Golgi maintenance
malfunction
disruption of inositol pentakisphosphate 2-kinase profoundly influences cellular processes
malfunction
in contrast to wild-type IPK1, which is able to restore the phosphate content of the ipk1-1 mutant to wild-type level, both kinase-inactive IPK1 forms fail to complement excessive phosphate accumulation and PSR gene activation in ipk1-1. Although both ipk1-1 and itpk1 mutants exhibit decreased levels of InsP6 (phytate) and diphosphoinositol pentakisphosphate (PP-InsP5; InsP7), disruption of another ITPK family enzyme, ITPK4, which correspondingly causes depletion of InsP6 and InsP7, does not display similar phosphate-related phenotypes, which precludes these InsP species from being effectors. Notably, the level of D/L-Ins(3,4,5,6)P4 is concurrently elevated in both ipk1-1 and itpk1 mutants, which demonstrates a specific correlation with the misregulated phosphate phenotypes. The level of D/L-Ins(3,4,5,6)P4 is not responsive to phosphate starvation that instead manifests a shoot-specific increase in the InsP7 level. Misregulation of phosphate homeostasis in ipk1-1 is not caused by defective InsP6-mediated mRNA export. Neither of the kinase-inactive IPK1 mutants K168A and D368A complement the PSR-like RSA phenotypes (i.e. reduced primary root and enhanced lateral root growth) of ipk1-1 mutant. In addition to the decreased InsP6 level, levels of InsP7 and InsP8 are also reduced in ipk1-1 mutants
malfunction
urine inositol pentakisphosphate 2-kinase and changes in kidney structure in early diabetic kidney disease in type 1 diabetes. A higher prevalence of detectable urinary inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPP2K) in type 1 diabetes correlates with early renal function decline. Proximal tubule cells from people with type 1 diabetes and diabetic kidney disease (DKD) express more IPP2K compared with controls. Demographics and clinical characteristics by tertile of baseline urine inositol 1,3,4,5,6-pentakisphosphate 2-kinase/creatinine (IPP2K/Cr), overview
malfunction
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cells lacking the enzyme display defects in dynein-dependent trafficking pathways including endosomal sorting, vesicle movement and Golgi maintenance
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metabolism
genetic dissection of the roles for InsP and PP-InsP biosynthesis enzymes in regulation of phosphate homeostasis, overview
metabolism
inositol 1,3,4,5,6-pentakisphosphate 2-kinase catalyzes the terminal step in the phytic acid biosynthetic pathway
metabolism
inositol tris/tetrakisphosphate kinase 1 (ITPK1, EC 2.7.1.134) and inositol pentakisphosphate 2-kinase (IPK1, EC 2.7.1.158) comprise a reversible metabolic cassette converting Ins(3,4,5,6)P4 into 5-InsP7 and back in a nucleotide-dependent manner. Ability of Arabidopsis inositol tris/tetrakisphosphate kinase 1 to discriminate between symmetric and enantiomeric substrates in the production of diverse symmetric and asymmetric myo-inositol phosphate and diphospho-myo-inositol phosphate (inositol diphosphate) products
metabolism
IPK1 is the terminal enzyme in phytic acid biosynthesis
metabolism
nositol 1,3,4,5,6-pentakisphosphate 2-kinase catalyzes the terminal step in the phytic acid biosynthetic pathway
physiological function
knock-out mutant cells are defective in nuclear mRNA export, cell morphology, polarized growth, and cell separation
physiological function
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Asp1 kinase activity regulates cell-cell adhesion and increases resistance towards thiabendazole. The Asp1 kinase activity encoded by the N-terminal part of the protein is regulated negatively by the C-terminal domain of Asp1. Asp1 is a key regulator of the morphological switch via the cAMP protein kinase A
physiological function
the enzyme activity is required for cytoplasmic dynein transport
physiological function
the enzyme has important roles in growth and phosphate homeostasis
physiological function
association of urine inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IPP2K) with the presence and progression of diabetic kidney disease (DKD) lesions. Inositol 6-phosphate is a key intracellular signaling molecule with roles in mRNA editing and chromatin remodeling
physiological function
GmIPK1 plays a significant role in phytate synthesis
physiological function
inositol 1,3,4,5,6-pentakisphosphate 2-kinase (IP5 2-K) phosphorylates inositol pentakisphosphate (IP5) to produce inositol 1,2,3,4,5,6-hexakisphosphate (IP6), from ATP
physiological function
inositol pentakisphosphate 2-kinase catalyzes the phosphorylation of the axial 2-OH of myo-inositol 1,3,4,5,6-pentakisphosphate for de novo synthesis of myo-inositol hexakisphosphate
physiological function
the kinase activity of inositol pentakisphosphate 2-kinase (IPK1) is required for phytate (inositol hexakisphosphate, InsP6) synthesis, and is indispensable for maintaining phosphate homeostasis under phosphate-replete conditions. Inositol 1,3,4-trisphosphate 5/6-kinase 1 (ITPK1) plays an equivalent role. In addition to regulating the phosphate content, the kinase activity of IPK1 is also required for root system architecture
physiological function
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the enzyme activity is required for cytoplasmic dynein transport
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additional information
molecular docking study
additional information
molecular docking study
additional information
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molecular docking study
additional information
overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
additional information
three-dimensional homolgy modelling, GmIPK1 protein model (PMD ID PM0079931), using Arabidopsis thaliana enzyme structure (PDB ID 4AQK) as template, structure-function relationship of GmIPK1, molecular dynamics simulations and molecular docking study, overview
additional information
three-dimensional homolgy modelling, GmIPK1 protein model (PMD ID PM0079931), using Arabidopsis thaliana enzyme structure (PDB ID 4AQK) as template, structure-function relationship of GmIPK1, molecular dynamics simulations and molecular docking study, overview
additional information
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three-dimensional homolgy modelling, GmIPK1 protein model (PMD ID PM0079931), using Arabidopsis thaliana enzyme structure (PDB ID 4AQK) as template, structure-function relationship of GmIPK1, molecular dynamics simulations and molecular docking study, overview
additional information
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overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
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additional information
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overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
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additional information
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overall structure analysis of enzyme CnIpk1, conformational state and changes, overview
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