Information on EC 2.7.1.134 - inositol-tetrakisphosphate 1-kinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.134
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RECOMMENDED NAME
GeneOntology No.
inositol-tetrakisphosphate 1-kinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1D-myo-inositol hexakisphosphate biosynthesis III (Spirodela polyrrhiza)
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D-myo-inositol (3,4,5,6)-tetrakisphosphate biosynthesis
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Inositol phosphate metabolism
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SYSTEMATIC NAME
IUBMB Comments
ATP:1D-myo-inositol-3,4,5,6-tetrakisphosphate 1-phosphotransferase
This enzyme also phosphorylates Ins(1,3,4)P3 on O-5 and O-6. The phosphotransfer from ATP to either inositol 1,3,4-trisphosphate or inositol 3,4,5,6-tetrakisphosphate appears to be freely reversible to the extent that the enzyme can act like an inositol polyphosphate phosphatase in the presence of ADP. It can also catalyse an isomerization between Ins(1,3,4,5)P4 and Ins(1,3,4,6)P4 in the presence of ADP.
CAS REGISTRY NUMBER
COMMENTARY hide
113356-25-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
108 accessions, gene itpk3-1
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
C57Bl6 mice
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Manually annotated by BRENDA team
L. var. indica, IR64
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Manually annotated by BRENDA team
Sprague-Dawley strain
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
ATP + D-myo-inositol 1,3,4-triphosphate
?
show the reaction diagram
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?
ATP + myo-inositol-1,3,4,6-tetrakisphosphate
ADP + myo-inositol-1,3,4,5-tetrakisphosphate
show the reaction diagram
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r
ATP + myo-inositol-1,3,4-trisphosphate
ADP + myo-inositol-1,2,3,4-tetrakisphosphate
show the reaction diagram
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minor product
?
ATP + myo-inositol-1,3,4-trisphosphate
ADP + myo-inositol-1,3,4,5-tetrakisphosphate
show the reaction diagram
ATP + myo-inositol-1,3,4-trisphosphate
ADP + myo-inositol-1,3,4,6-tetrakisphosphate
show the reaction diagram
ATP + myo-inositol-3,4,6-trisphosphate
ADP + myo-inositol-1,3,4,6-tetrakisphosphate
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + 1D-myo-inositol 3,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
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activation at 0.0001 mM, 10-20% inhibition at 0.001 mM Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
inositol 1,2,3,6-tetrakisphosphate
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strong nonspecific inhibition
inositol 1,2,5,6-tetrakisphosphate
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strong nonspecific inhibition
inositol 1,3,4-trisphosphate
inositol-1,3,4,5,6-pentakisphosphate
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competitive inhibition
Inositol-1,3,4,5-tetrakisphosphate
Inositol-1,3,4,6-tetrakisphosphate
inositol-1,4,5-trisphosphate
inositol-hexakisphosphate
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0.1 mM, almost complete inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
inositol-1,3,4-trisphosphate
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activation of inositol-1,3,4,5,6-phosphate 1-phosphatase activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.01 - 0.17
ATP
0.0003 - 0.2
myo-inositol-1,3,4-trisphosphate
0.0001 - 0.00036
myo-inositol-3,4,5,6-tetrakisphosphate
0.0002
myo-inositol-3,4,6-trisphosphate
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pH 7.2, 37C, recombinant enzyme
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.015
Inositol 1,3,4,5,6-pentakisphosphate
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pH 7.2, 37C
0.009
Inositol 1,3,4,5-tetrakisphosphate
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pH 7.2, 37C
0.015
Inositol 1,3,4,6-tetrakisphosphate
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pH 7.2, 37C
0.0002
inositol 1,3,4-trisphosphate
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pH 7.2, 37C
0.048
Inositol 1,4,5-trisphosphate
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pH 7.2, 37C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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specific activities of various rat tissues
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
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deduced from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
very low expression level
Manually annotated by BRENDA team
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permeabilized
Manually annotated by BRENDA team
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3.6 kilobases transcript detected by Northern blot
Manually annotated by BRENDA team
very low expression level
Manually annotated by BRENDA team
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3.6 kilobases transcript detected by Northern blot
Manually annotated by BRENDA team
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bone marrow
Manually annotated by BRENDA team
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3.6 kilobases transcript detected by Northern blot
Manually annotated by BRENDA team
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3.6 kilobases transcript detected by Northern blot
Manually annotated by BRENDA team
very low expression level
Manually annotated by BRENDA team
very low expression level
Manually annotated by BRENDA team
additional information
expression pattern of isozyme ITPK2, no or very poor expression in stem
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
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brain enzyme, gel filtration
47000
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x * 47000, deduced from nucleotide sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
10 mM sodium diphosphate stabilizes ammonium sulfate precipitated enzyme, no loss of activity after 2 days at 4C
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, 1 mg/ml bovine serum albumin, 20% glycerol, 6 months, no loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, brain enzyme
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by chromatography on a glutathione agarose column
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heparin-agarose, affinity elution with inositol hexakisphosphate, Mono Q
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heparin-agarose, phenyl-Sepharose, Mono Q Matrex Blue A
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polyethyleneimine, DEAE Toyopearl 650M
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a recombinant fusion protein between GST and residues 124-311 of human ITPK1 is prepared in Escherichia coli to produce antibodies for Western blotting
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expressed in Escherichia coli
expression in colonic epithelial T84 cells
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expression in Escherichia coli
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expresssion in Escherichia coli
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gene ITPK2, expression analysis of wild-type and mutant enzymes by quantitative real-time PCR analysis
gene itpk3-1, genotyping, 108 different accessions, the Arabidopsis accessions differ in their response to Zn deficiency, quantitative real-time PCR enzyme expression anaysis, overview
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H162D
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loss-of-function for Ins(1,3,4)P3 in the H162D mutant is matched by a 200fold reduction in its Ins(1,3,4)P3 kinase activity. The H162D mutant dephosphorylats Ins(1,3,4,5,6)P5 almost twice as fast as the wild-type enzyme. The H162D mutant also displays very limited ability to transfer phosphate from Ins(1,3,4,5,6)P5 to Ins(1,3,4)P3 in the presence of physiological concentrations of nucleotide
S356N
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same catalytic activity as wild-type
additional information
Show AA Sequence (465 entries)
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