Information on EC 2.7.1.151 - inositol-polyphosphate multikinase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.7.1.151
-
RECOMMENDED NAME
GeneOntology No.
inositol-polyphosphate multikinase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho-group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
1D-myo-inositol hexakisphosphate biosynthesis I (from Ins(1,4,5)P3)
-
-
1D-myo-inositol hexakisphosphate biosynthesis V (from Ins(1,3,4)P3)
-
-
D-myo-inositol (1,4,5,6)-tetrakisphosphate biosynthesis
-
-
Inositol phosphate metabolism
-
-
NIL
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP:1D-myo-inositol-1,4,5-trisphosphate 6-phosphotransferase
This enzyme also phosphorylates Ins(1,4,5)P3 to Ins(1,3,4,5)P4, Ins(1,3,4,5)P4 to Ins(1,3,4,5,6)P5, and Ins(1,3,4,5,6)P4 to Ins(PP)P4, isomer unknown. The enzyme from the plant Arabidopsis thaliana can also phosphorylate Ins(1,3,4,6)P4 and Ins(1,2,3,4,6)P5 at the D-5-position to produce 1,3,4,5,6-pentakisphosphate and inositol hexakisphosphate (InsP6), respectively [3]. Yeast produce InsP6 from Ins(1,4,5)P3 by the actions of this enzyme and EC 2.7.1.158, inositol-pentakisphosphate 2-kinase [4].
CAS REGISTRY NUMBER
COMMENTARY hide
9077-69-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Like the yeast enzyme, mammalian, plant and fly orthologs share the capacity for the conversion of Ins(1,4,5)P3 to Ins(1,3,4,5,6)P5. Plant and fly IPMKs recapitulate the yeast enzyme's preference for D6-hydroxyl phoshorylation followed by D3-hydroxylphosphorylation, mammalian IPMKs appear to prefer the reverse order.
-
-
Manually annotated by BRENDA team
white leghorn chick
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-
Manually annotated by BRENDA team
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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
2 ATP + 1D-myo-inositol 1,4,5-trisphosphate
2 ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
2 ATP + 1D-myo-inositol 4,5-bisphosphate
2 ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
show the reaction diagram
-
-
-
-
?
3 ATP + 2 1D-myo-inositol 1,4,5-trisphosphate
3 ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate
ADP + diphosphoinositol pentakisphosphate
show the reaction diagram
-
isozyme Kcs1
-
-
?
ATP + 1D-myo-inositol 1,2,3,4,6-pentakisphosphate
ADP + 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate
show the reaction diagram
-
-
-
?
ATP + 1D-myo-inositol 1,2,3,4,6-pentakisphosphate
ADP + inositol hexakisphosphate
show the reaction diagram
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + diphosphoinositol tetrakisphosphate
show the reaction diagram
-
isozyme Kcs1
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ADP + ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
-
-
-
-
r
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
show the reaction diagram
-
2fold less active compared to 1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
-
?
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
show the reaction diagram
ATP + inositol 1,3,4,5-tetrakisphosphate
ADP + inositol (1,3,4,5,6)-pentakisphosphate
show the reaction diagram
-
substrate preference for inositol 1,3,4,6-tetrakisphosphate over inositol 1,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate
-
-
?
ATP + inositol 1,4,5,6-tetrakisphosphate
ADP + inositol (1,3,4,5,6)-pentakisphosphate
show the reaction diagram
ATP + inositol 1,4,5-trisphosphate
ADP + inositol (1,3,4,5)-tetrakisphosphate
show the reaction diagram
-
substrate preference for inositol 1,3,4,6-tetrakisphosphate over inositol 1,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate
-
-
?
ATP + phosphatidylinositol 4,5-bisphosphate
ADP + phosphatidylinositol (3,4,5)-trisphosphate
show the reaction diagram
-
-
-
-
?
ATP + phosphatidylinositol 4,5-bisphosphate
ADP + phosphatidylinositol 3,4,5-trisphosphate
show the reaction diagram
-
in rats
-
-
?
inositol (1,3,4,5)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
show the reaction diagram
-
no inositol (1,2,4,5,6) pentakisphosphate is formed
-
?
inositol (1,3,4,5)-tetrakisphosphate + ATP
inositol pentakisphosphate + ADP
show the reaction diagram
-
-
?
inositol (1,3,4,6)-tetrakisphosphate + ATP
ADP + inositol (1,3,4,5,6)-pentakisphosphate
show the reaction diagram
-
substrate preference for inositol 1,3,4,6-tetrakisphosphate over inositol 1,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate
-
-
?
inositol (1,4,5)-triphosphate + ATP
inositol (1,3,4,5)-tetrakisphosphate + ADP
show the reaction diagram
-
-
?
inositol (1,4,5)-triphosphate + ATP
inositol (1,3,4,5)-tetrakisphosphate + inositol (1,4,5,6)-tetrakisphosphate + ADP
show the reaction diagram
-
-
-
?
inositol (1,4,5,6)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
show the reaction diagram
inositol (3,4,5,6)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
show the reaction diagram
-
hITPK1 has more than 13000fold preference for inositol (3,4,5,6)-tetrakisphosphate over its enantiomer inositol (1,4,5,6)-tetrakisphosphate
-
-
?
inositol (4,5)-bisphosphate + ATP
inositol (1,4,5)-trisphosphate + ADP
show the reaction diagram
-
-
?
inositol bisphosphate + ATP
inositol trisphosphate + ADP
show the reaction diagram
-
-
-
?
inositol monophosphate + ATP
inositol diphosphate + ADP
show the reaction diagram
-
-
-
?
inositol pentakisphosphate + ATP
diphosphoinositol tetrakisphosphate + ADP
show the reaction diagram
-
-
?
inositol pentakisphosphate + ATP
inositol hexakisphosphate + ADP
show the reaction diagram
inositol tetrakisphosphate + ATP
inositol pentakisphosphate + ADP
show the reaction diagram
-
-
-
?
myo-inositol tetrakisphosphate + ATP
myo-inositol pentakisphosphate + ADP
show the reaction diagram
myo-inositol triphosphate + ATP
myo-inositol tetrakisphosphate + ADP
show the reaction diagram
additional information
?
-
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
2 ATP + 1D-myo-inositol 1,4,5-trisphosphate
2 ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
-
-
-
-
r
2 ATP + 1D-myo-inositol 4,5-bisphosphate
2 ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
show the reaction diagram
-
-
-
-
?
3 ATP + 2 1D-myo-inositol 1,4,5-trisphosphate
3 ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 1,2,3,4,5,6-hexakisphosphate
ADP + diphosphoinositol pentakisphosphate
show the reaction diagram
-
isozyme Kcs1
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-
?
ATP + 1D-myo-inositol 1,2,3,4,6-pentakisphosphate
ADP + inositol hexakisphosphate
show the reaction diagram
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
ADP + diphosphoinositol tetrakisphosphate
show the reaction diagram
-
isozyme Kcs1
-
-
?
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
-
-
-
-
ir
ATP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate + 1D-myo-inositol 1,4,5,6-pentakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
-
-
-
-
?
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate
ADP + ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
-
-
-
-
r
ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 1,4,5-trisphosphate
ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
show the reaction diagram
ATP + 1D-myo-inositol 4,5-bisphosphate
ADP + 1D-myo-inositol 3,4,5-trisphosphate
show the reaction diagram
ATP + inositol 1,4,5,6-tetrakisphosphate
ADP + inositol (1,3,4,5,6)-pentakisphosphate
show the reaction diagram
-
stable over-expression of the human protein in HEK-293 cells abrogates the in vivo elevation of inositol 1,4,5,6-tetrakisphosphate from the Salmonella dublin SopB protein. The enzyme may play a role in regulation of the level of inositol 1,4,5,6-tetrakisphosphate in human cells
-
-
?
ATP + phosphatidylinositol 4,5-bisphosphate
ADP + phosphatidylinositol (3,4,5)-trisphosphate
show the reaction diagram
-
-
-
-
?
ATP + phosphatidylinositol 4,5-bisphosphate
ADP + phosphatidylinositol 3,4,5-trisphosphate
show the reaction diagram
-
in rats
-
-
?
inositol (1,4,5,6)-tetrakisphosphate + ATP
inositol (1,3,4,5,6)-pentakisphosphate + ADP
show the reaction diagram
-
inositol polyphosphate multikinase is a key mediators in the production of inositol (1,3,4,5,6)-pentakisphosphate
-
-
?
myo-inositol triphosphate + ATP
myo-inositol tetrakisphosphate + ADP
show the reaction diagram
-
it appears that the enzyme utilizes inositol triphosphate as the initial substrate for the synthesis of higher myo-inositol polyphosphates
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
free enzyme and inhibited enzyme are not affected by Ca2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
abscisic acid
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In ten-day-old seedlings grown on MS medium, AtIpk2b transcript level decreased.
aurintricarboxylic acid
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate, strong inhibition, IC50 is 44 nM
chlorogenic acid
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate, slight inhibition, IC50 is 0.0012 mM
ellagic acid
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate, slight inhibition, IC50 is 0.0014 mM
gossypol
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate, slight inhibition, IC50 is 0.0034 mM
inositol(1,3,4)-trisphosphate
-
potently inhibits hITPK1 activity towards insositol (3,4,5,6)-tetrakisphosphate, IC50: 0.0076 mM
inositol(3,5,6)-trisphosphate
-
IC50: 0.1 mM
NaCl
-
In ten-day-old seedlings grown on MS medium, AtIpk2b transcript level decreases in response to salt
Rose bengal
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate, slight inhibition, IC50 is 620 nM
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
indole-3-acetic acid
The expression of AtIpk2b is enhanced in roots after treatment with 1 microM. Expression of AtIpk2b become stronger when the concentration of exogenous indole-3-acetic acid is increased to 10 microM. By treatment with 40 microM, AtIpk2b expression increases after 0.5 h of treatment, whereas the expression of AtIpk2a remains virtually unaffected. These results indicate that AtIpk2b is an IAA-inducible gene, while AtIpk2a is not.
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00013 - 0.568
1D-myo-inositol 1,3,4,5-tetrakisphosphate
0.0003
1D-myo-inositol 1,3,4,6-tetrakisphosphate
-
recombinant enzyme, pH 7.2, 37°C
0.00022 - 0.254
1D-myo-inositol 1,4,5,6-tetrakisphosphate
0.00011 - 0.162
1D-myo-inositol 1,4,5-trisphosphate
0.006 - 0.03
1D-myo-inositol 4,5-bisphosphate
0.000222
1D-myo-inositol-1,4,5,6-tetrakisphosphate
-
37°C, pH 7.2
0.017 - 0.039
ATP
0.000129
inositol (1,3,4,5)-tetrakisphosphate
-
37°C, pH 7.2
0.000295
inositol (1,3,4,6)-tetrakisphosphate
-
37°C, pH 7.2
0.000112
inositol (1,4,5)-trisphosphate
-
37°C, pH 7.2
0.00018
inositol (1,4,5,6)-tetrakisphosphate
-
-
additional information
additional information
-
kinetics
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.8 - 106
1D-myo-inositol 1,3,4,5-tetrakisphosphate
3051
0.97 - 79.1
1D-myo-inositol 1,4,5,6-tetrakisphosphate
5299
29.7 - 37.8
1D-myo-inositol 1,4,5-trisphosphate
1583
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00015
inositol (1,3,4)-trisphosphate
-
-
0.002
inositol (3,5,6)-trisphosphate
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000044
aurintricarboxylic acid
Homo sapiens
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate, strong inhibition, IC50 is 44 nM
0.0012
chlorogenic acid
Homo sapiens
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate, slight inhibition, IC50 is 0.0012 mM
0.0014
ellagic acid
Homo sapiens
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate, slight inhibition, IC50 is 0.0014 mM
0.0034
gossypol
Homo sapiens
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate, slight inhibition, IC50 is 0.0034 mM
0.0076
inositol(1,3,4)-trisphosphate
Homo sapiens
-
potently inhibits hITPK1 activity towards insositol (3,4,5,6)-tetrakisphosphate, IC50: 0.0076 mM
0.1
inositol(3,5,6)-trisphosphate
Homo sapiens
-
IC50: 0.1 mM
0.00062
Rose bengal
Homo sapiens
-
mixed-type versus ATP, noncompetitive versus 1D-myo-inositol 1,4,5-trisphosphate, slight inhibition, IC50 is 620 nM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0085
-
-
0.37
-
substrate inositol monophosphate
0.45
purified recombinant enzyme, 1D-myo-inositol 1,3,4,5,6-pentakisphosphate formation from 1D-myo-inositol 1,4,5-trisphosphate, 0.5 mM ATP
0.49
-
substrate inositol diphosphate
0.5
-
partially purified enzyme
0.7
-
partially purified enzyme
1.84
-
substrate inositol triphosphate
1.92
-
substrate inositol tetrakisphosphate
2.5
-
recombinant wild-type enzyme, substrate 1D-myo-inositol 1,4,5-trisphosphate
3.08
-
substrate inositol pentakisphosphate
5.5
-
recombinant deletion mutant enzyme, substrate 1D-myo-inositol 1,4,5-trisphosphate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
7.8
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
erythrocyte
Manually annotated by BRENDA team
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; derived from wild-type and mutant zygotes
Manually annotated by BRENDA team
most highly expressed
Manually annotated by BRENDA team
-
isozyme Ipk2beta
Manually annotated by BRENDA team
-
isozyme Ipk2beta
Manually annotated by BRENDA team
-
from Huntington's disease patients and healthy persons, severe loss of IPMK in the striatum of Huntington's disease patients
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
-
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33000
-
calculated and confirmed by Western Blot analysis
44000
-
x * 44000, SDS-PAGE
44400
x * 44400, deduced from nucleotide sequence
47219
x * 47219, amino acid sequence calculation
58000
-
4 * 58000, SDS-PAGE
234000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
-
4 * 58000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
additional information
-
the enzyme can be phosphorylated by protein kinase C in vitro
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isoform inositol phosphate multikinase alpha, to 2.9 A resolution. The structural core of Arabidopsis thaliana IPMK is homologous to those of Saccharamyces cerevisiae IPMK and Homo sapiens IP3K
sitting drop vapor diffusion method. Crystal structure of the yeast inositol phosphate multikinase Ipk2 in the apoform and in a complex with ADP and Mn2+ at up to 2.0 A resolution
-
Structure database comparisons of the recently solved crystal strucures of Ins(1,4,5)P3-kinase and IPMK confirm the close structural relationship to the lipid inositol kinases despite little primary amino acid sequence similarities.
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
1 min, inactivation, purified recombinant isozyme; 1 min, inactivation, purified recombinant isozyme
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
2-mercaptoethanol or other -SH containing compounds protect the enzyme
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
enzyme is not affected by 3% v/v DMSO
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, Con A-Sepharose, DEAE-Toyopearl, 5'AMP-Sepharose
-
ammonuium sulfate, DEAE-cellulose
-
native enzyme partially by nuclear fraction preparation
recombinant enzyme
-
recombinant enzyme from Escherichia coli strain BL21(DE3) to near homogeneity by ion exchange and phosphocellulose resin chromatography
recombinant enzyme from strain expression in strain 12S16cpep4D by nickel affinity chromatography
-
recombinant GST-fusion isozymes from Escherichia coli by glutathione affinity chromatography; recombinant GST-fusion isozymes from Escherichia coli by glutathione affinity chromatography
recombinant N-terminally His-tagged enzyme from Escherichia coli strain BL21(DE3) by cobalt affinity chromatography
-
recombinant wild-type enzyme and deletion mutant from Escherichia coli by ion exchange and phosphocellulose resin chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, no functional complementation of yeast mutant strains, expression of the N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
DNA and amino acid sequence determination and analysis, overexpression as C-terminally GFP-tagged fusion protein in Escherichia coli strain BL21(DE3), transient expression in NRK 52E cells as C- or N-terminally GFP-tagged fusion protein
Examinations of plants deficient in IPMK suggest roles in pollen germination, root growth, as well axillary shoot branching.
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expressed in Lycopersicon esculentum cv. PKM
expression in bacteria as glutathione S-transferase fusion protein
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expression in enzyme-deficient yeast cells, stable overexpression in HEK-293 cells, abrogates the in vivo elevation of 1D-myo-inositol 1,4,5,6-tetrakisphosphate from the Salmonella dublin SopB protein
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expression in HEK293 cells as glutathione S-transferase fusion protein
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expression in Saccharomyces cerevisiae. A lysine accumulation phenotype of ScIpk2DELTA mutant yeast is rescued by Solanum tuberosum inositol phosphate multikinase
Expression of AtIpk2b in yeast mutant arg82D, quantitative real-time PCR analysis of AtIpk2b expression in Arabidopsis. AtIpk2b cDNA containing the complete open reading frame is inserted via XbaI-SalI sites into the binary vector pBinAR-HPT. Resulting construct is introduced into Agrobacterium tumefaciens (strain LBA4404). Tobacco leaf disks are infected with the transformed Agrobacteria.
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expression of HA-tagged enzyme in human HEK293 and in COS-7 cells
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expression of wild-type enzyme and deletion mutant in Escherichia coli
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gene impk, adeno-associated virus serotype 2-mediated delivery of IPMK into mouse brain, in the striatum of R6/2 Huntington's disease mice
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gene impk, recombinant GST-tagged IMPK overexpression in human colon cancer cell line HCT-116 and the human osteosarcoma cell line U2-OS. Overexpression of kinase-deficient IPMK inhibits cell proliferation in etoposide-treated U2OS cells to a similar extent as does wild-type IPMK
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gene ipk2 is located on chromosome 10
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gene KCS1, subcloning in Escherichia coli strain XL1-B, overexpression in strain arg82DELTA, expression in strain 12S16cpep4D
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genetic map of inositol metabolism, overexpression of isozyme Kcs1 can complement isozyme Ipk2 deficiency
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His-tagged enzyme, expression in Escherichia coli
IPMK knockout mice demonstrates the critical roles of IPMK in embryogenesis and central nevous system development. Deletion of IPMK in mice results in early lethality.
isozyme Ipk2alpha, location on chromosome 5, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant isozyme in Escherichia coli with or without GST-fusion tag, functional complementation of an enzyme-deficient yeast strain; isozyme Ipk2beta, location on chromosome 5, DNA and amino acid sequence determination and analysis, expression of wild-type and mutant isozyme in Escherichia coli with or without GST-fusion tag, functional complementation of an enzyme-deficient yeast strain
Observed derepression and constitutive elevated levels levels of the transcripts in IPMK mutant yeast but not in ipk1- or ipk6-deficient yeasts confirms the requirement of IPMK in the transcriptional regulation of arginine anabolism and catabolism.; While wild-type yeast displays sequential phosphorylation of Ins(1,4,5)P3 to Ins6, mutation of locus termed GSL3 resulted in the loss of Ins(1,4,5)P3-initiated higher isnositol polyphosphate metabolism. IPMK is identified as GSL3 (Ipk2) and confirmed its requirement for mRNA export.
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overexpressed in Escherichia coli strain BL21Star
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To create an AtIpk2b overexpression construct, the AtIpk2b cDNA is cut from plasmid pmIP3K with XbaI-XhoI and inserted via XbaI-SalI sites into pBinAR-HPT vector behind the cauliflower mosaic virus 35S promoter. The resulting plasmid is first introduced into Agrobacterium tumefaciens by electroporation and then transformed Arabidopsis ecotype C24 by vacuum infiltration. Transgenic plants are selected on MS medium containing 20 mg/L hygromycin. Eleven AtIpk2b overexpression plants, named OX-2, OX-3, OX-5, OX-8, OX-9, OX-15, OX-25, OX-26, OX-33, OX-35, and OX-64, are identified. Compared to the wild type, branching of axillary shoots is more pronounced in the overexpression lines.
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D100A
isozyme IPK2beta, site-directed mutagenesis, inactive mutant
D98A
isozyme IPK2alpha, site-directed mutagenesis, inactive mutant
K117W
mutant exhibits nearly normal 6-kinase function but harbors significantly reduced 3-kinase activity. The mutant complements conditional nutritional growth defects observed in ipmk null yeast and suppresses lethality observed in ipmk null flies
K117W/K121W
mutant exhibits nearly normal 6-kinase function but harbors significantly reduced 3-kinase activity. The mutant complements conditional nutritional growth defects observed in ipmk null yeast and suppresses lethality observed in ipmk null flies
K121W
although no inositol tetrakisphosphate is present with wild-type IPMK, levels of inositol tetrakisphosphate and inositol hexakisphosphate are equivalent in mutant K121W
D144N
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site-directed mutagenesis
D144N/K146A
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site-directed mutagenesis
K129A/S235A
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catalytically inactive mutant
K146A
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site-directed mutagenesis
K327Q/K328Q
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site-directed mutagenesis, generation of an IPMK mutant with inactivated nuclear localization signal, NLS, whose intracellular distribution is unaffected by inhibition of conventional protein import
L794A/L801A
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site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, phenotype overview
L794A/L801A/L857A/L864A
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site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, the mutant strain shows compromised cell wall integrity, phenotype overview
L857A/L864A
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site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, phenotype overview
S887A/L888A/L889A
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site-directed mutagenesis, expression in the knockout mutant strain results in activity similar to the wild-type enzyme, the mutant strain shows compromised cell wall integrity, phenotype overview
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
transgenic tomato plants show increased tolerance to drought, cold and oxidative stress
medicine
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