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1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP
1D-myo-inositol hexakisphosphate + ADP
intermediate in both lipid-dependent and lipid-independent phytic acid biosynthetic pathways
phytic acid, in higher plants, phytic acid can mediate abscisic acid-induced guard cell closure by inactivating plasma membrane inward K+ conductance. During this process, phytic acid appears to act as an endomembrane calcium-releasing signal.
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1D-myo-inositol 1,4,6-trisphosphate + ATP
1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
relative substrate specificity 93.9%
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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ATP + 1D-myo-inositol 1,4,6-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
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ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
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ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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ATP + myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + myo-inositol hexakisphosphate
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ATP + myo-inositol 1,4,6-trisphosphate
ADP + inositol 1,2,4,6-tetrakisphosphate
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additional information
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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the enzyme may be involved in both inositol hexakisphosphate formation in maturing seeds and ATP resynthesis in germinating seeds
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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it is suggested that the enzyme is necessary for yolk sac development or function. Loss of inositol 1,3,4,5,6-pentakisphosphate 2-kinase is lethal
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
rate-determining step in production of 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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cytoplasmic production of 1D-myo-inositol hexakisphosphate is sufficient for mediating the Gle1-mRNA export pathway
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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the product 1D-myo-inositol hexakisphosphate plays a role in messenger RNA export
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
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ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol hexakisphosphate
the predominant activity of StITPK1 is that of an InsP5-ADP phosphotransferase.
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ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
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ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
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ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
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low activity
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additional information
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no activity with 1D-myo-inositol 1,3,4,5-tetrakisphosphate
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additional information
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phosphotransfer from 2-FAM-InsP5 (2-O-(2-(5-fluoresceinylcarboxy)aminoethyl)-myo-inositol 1,3,4,5,6-pentakisphosphate) to ADP by AtIP5 2-K
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additional information
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with inositol tris/tetrakisphosphate kinase 1 (ITPK1, EC 2.7.1.134) and inositol pentakisphosphate 2-kinase (IPK1, EC 2.7.1.158) combined at a 1:20 ATP:ADP ratio, InsP6 is converted via Ins(1,3,4,5,6)P5 to Ins(3,4,5,6) P4 and/or Ins(1,4,5,6)P4 with concomitant generation of ATP
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additional information
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substrate binding structure, overview
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additional information
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substrate binding structure, overview
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additional information
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substrate binding structure, overview
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additional information
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substrate binding structure, overview
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additional information
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binding sites of ADP and IP6 are observed to be present side by side with few common interacting amino acid residues: R193, K171. The residues that are making interactions with ADP include W130, K171, R193, H197, K201, Q204, and N239, whereas the residues that are making interactions with IP6 include G17, E18, G19, A20, N22, L23, V24, R40, K43, R131, R169, K171, R193, R242, and S373
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additional information
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binding sites of ADP and IP6 are observed to be present side by side with few common interacting amino acid residues: R193, K171. The residues that are making interactions with ADP include W130, K171, R193, H197, K201, Q204, and N239, whereas the residues that are making interactions with IP6 include G17, E18, G19, A20, N22, L23, V24, R40, K43, R131, R169, K171, R193, R242, and S373
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additional information
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binding sites of ADP and IP6 are observed to be present side by side with few common interacting amino acid residues: R193, K171. The residues that are making interactions with ADP include W130, K171, R193, H197, K201, Q204, and N239, whereas the residues that are making interactions with IP6 include G17, E18, G19, A20, N22, L23, V24, R40, K43, R131, R169, K171, R193, R242, and S373
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additional information
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the enzyme changes its kinase activity towards 1D-myo-inositol hexakisphosphate at a decreasing ATP/ADP ratio to an ADP phosphotransferase activity and dephosphorylate 1D-myo-inositol hexakisphosphate
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additional information
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loss of the 2-kinase is lethal
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additional information
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mIP5 2-K active site and substrate recognition, overview. The adenine is strongly recognized through polar and hydrophobic interactions with both protein lobes and the hinge connecting them. In particular, it forms polar interactions with His14 and the backbones of Pro116 and Leu118. The ribose OHs interact with the C-lobe residues Glu136 and Arg209. The triphosphate moiety is tightly bound to the N-lobe of the enzyme through polar interactions and to the C-lobe through two magnesium ions. In particular, phosphate interaction with residue Arg-33, with a flexible loop (G-loop, residues Gly15-Ser20) and with an acidic residue (Asp437) through the magnesium ions, is conserved throughout the PK superfamily and is essential for nucleotide binding and kinase activity
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additional information
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mIP5 2-K active site and substrate recognition, overview. The adenine is strongly recognized through polar and hydrophobic interactions with both protein lobes and the hinge connecting them. In particular, it forms polar interactions with His14 and the backbones of Pro116 and Leu118. The ribose OHs interact with the C-lobe residues Glu136 and Arg209. The triphosphate moiety is tightly bound to the N-lobe of the enzyme through polar interactions and to the C-lobe through two magnesium ions. In particular, phosphate interaction with residue Arg-33, with a flexible loop (G-loop, residues Gly15-Ser20) and with an acidic residue (Asp437) through the magnesium ions, is conserved throughout the PK superfamily and is essential for nucleotide binding and kinase activity
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additional information
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the enzyme changes its kinase activity towards 1D-myo-inositol hexakisphosphate at a decreasing ATP/ADP ratio to an ADP phosphotransferase activity and dephosphorylate 1D-myo-inositol hexakisphosphate
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additional information
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StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate-ADP phosphotransferase activity in presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity.
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additional information
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StITPK1 displays inositol 3,4,5,6-tetrakisphosphate 1-kinase activity. The enzyme displays inositol 1,3,4,5,6-pentakisphosphate 1-phosphatase activity in the absence of a nucleotide acceptor and inositol 1,3,4,5,6-pentakisphosphate-ADP phosphotransferase activity in presence of physiological concentrations of ADP. Additionally, StITPK1 shows inositol phosphate-inositol phosphate phosphotransferase activity.
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additional information
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capable to catalyze the phosphorylation of myo-inositol 1,4,5,6-tetrakisphosphate (relative substrate specificity 76.8%), and myo-inositol 3,4,5,6-tetrakisphosphate (relative substrate specificity 32.6%)
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additional information
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capable to catalyze the phosphorylation of myo-inositol 1,4,5,6-tetrakisphosphate (relative substrate specificity 76.8%), and myo-inositol 3,4,5,6-tetrakisphosphate (relative substrate specificity 32.6%)
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additional information
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capable to catalyze the phosphorylation of myo-inositol 1,4,5,6-tetrakisphosphate (relative substrate specificity 76.8%), and myo-inositol 3,4,5,6-tetrakisphosphate (relative substrate specificity 32.6%)
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