2.7.1.127: inositol-trisphosphate 3-kinase
This is an abbreviated version!
For detailed information about inositol-trisphosphate 3-kinase, go to the full flat file.
Word Map on EC 2.7.1.127
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2.7.1.127
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1,3,4,5-tetrakisphosphate
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kawasaki
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vasculitis
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5-phosphatase
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tetrakisphosphate
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diagnostics
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medicine
- 2.7.1.127
- 1,3,4,5-tetrakisphosphate
- kawasaki
-
vasculitis
-
5-phosphatase
-
tetrakisphosphate
- diagnostics
- medicine
Reaction
Synonyms
1D-myo-inositol-trisphosphate 3-kinase, Arg82, ArgRIII, D-myo-inositol 1,4,5-trisphosphate 3-kinase, GsIP3K-A, HsIP3K-A, inositol (1,4,5) trisphosphate 3 kinase B, inositol (1,4,5) trisphosphate 3-kinase, inositol 1,4,5-trisphosphate 3-kinase, inositol 1,4,5-trisphosphate 3-kinase A, inositol 1,4,5-trisphosphate 3-kinase B, inositol 1,4,5-trisphosphate 3-kinase C, inositol 1,4,5-trisphosphate 3-kinases, inositol 1,4,5-trisphosphate kinase, inositol 1,4,5-trisphosphate kinase 2, inositol 1,4,5-trisphosphate-3-kinase-A, inositol polyphosphate multikinase, inositol trisphosphate 3-kinase B, inositol(1,4,5)P3 3-kinase, inositol(1,4,5)trisphosphate 3-kinase, inositol(1,4,5)trisphosphate 3-kinases, inositol-1,4,5-trisphosphate 3-kinase, inositol-1,4,5-trisphosphate 3-kinase A, inositol-1,4,5-trisphosphate 3-kinase-A, inositol-1,4,5-trisphosphate-3-kinase, inositol-1,4,5-trisphosphate-3-kinase A, inositol-1,4,5-trisphosphate-3-kinase-A, inositol-trisphosphate 3-kinase B, Ins(1,4,5)P(3) 3-kinase B, Ins(1,4,5)P3 3-kinase, Ins(1,4,5)P3 3-kinase isoform B, Ins(1,4,5)P3 kinase, InsP3 3-kinase, InsP3 3-kinase A, InsP3 3-kinase B, InsP3 3-kinase C, InsP3K, InsP3KB, InsP3Kinase, IP3 3-kinase, IP3 3-kinase 2, IP3-3K, IP3K, IP3K-A, IP3K-B, IP3K-C, IP3K1, IP3K2, IP3KA, IP3KB, IP3KC, IP3kin, Ipk2, IPMK, ITPKA, Itpkb, Itpkc, kinase (phosphorylating), inositol 1,4,5-trisphosphate 3-, More, RnIP3K-C, wavy
ECTree
2.7.1.127 inositol-trisphosphate 3-kinaseAdvanced search results
results (
results (IC50 Value
IC50 Value on EC 2.7.1.127 - inositol-trisphosphate 3-kinase
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IC50 VALUE [mM] 
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.156
(2'S)-1D-1,2-O-[(2'-phosphoryloxy)propane-1',3'-diyl]-myo-inositol 4,5-bisphosphate
Rattus norvegicus
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synthetic bicyclic inositol trisphosphate S epimer, IC50 is 0.156 mM
0.013
1D-myo-inositol 1,3,4,5-tetrakisphosphate
Rattus norvegicus
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product inhibition, IC50 is 0.013 mM
0.000157
2-[3,5-dimethyl-1-(4-nitrophenyl)-1H-pyrazol-4-yl]-5,8-dinitro-1H-benzo[de]isoquinoline-1,3(2H)-dione
Homo sapiens
pH and temperature not specified in the publication
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0.036
7-methylsulfanyl-3-phenyl-[1,3,4]thiadiazolo[2,3-c][1,2,4]triazin-4-one
Homo sapiens
pH 7.5, 30°C, recombinant enzyme
0.0054
D-2-deoxyinositol 1,3,4,5-tetrakisphosphate
Rattus norvegicus
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strong inhibition of isozyme A, IC50 is 0.0054 mM
0.0017
D-2-deoxyinositol 1,4,5-trisphosphate
Rattus norvegicus
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strong inhibition of isozyme A, IC50 is 0.0017 mM
0.0014
D-3-deoxyinositol 1,4,6-trisphosphate
Rattus norvegicus
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strong inhibition of isozyme A, IC50 is 0.0014 mM
0.0051
D-6-deoxyinositol 1,3,4,5-tetrakisphosphate
Rattus norvegicus
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strong inhibition of isozyme A, IC50 is 0.0051 mM
0.003
D-myo-inositol 1,4,5-trisphosphate
Rattus norvegicus
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strong inhibition, purified recombinant enzyme, IC50 value is 0.003 mM in absence of Ca2+
0.1
D-scyllo-inositol 1,2,3,4-tetrakisphosphate
Rattus norvegicus
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purified recombinant enzyme, IC50 value is above 0.1 mM in absence of Ca2+
0.044
D-scyllo-inositol 1,2,4-trisphosphate
Rattus norvegicus
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purified recombinant enzyme, IC50 value is 0.044 mM in absence of Ca2+
0.1
L-scyllo-inositol 1,2,3,4-tetrakisphosphate
Rattus norvegicus
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purified recombinant enzyme, IC50 value is above 0.1 mM in absence of Ca2+
0.006
L-scyllo-inositol 1,2,4-trisphosphate
Rattus norvegicus
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purified recombinant enzyme, IC50 value is 0.006 mM in absence of Ca2+
0.037
N-(1,2-benzoxazol-3-yl)-4-methylbenzamide
Homo sapiens
pH 7.5, 30°C, recombinant enzyme
0.017
N-(4-ethoxyphenyl)pyrazolo[1,5-a]pyridine-3-carboxamide
Homo sapiens
pH 7.5, 30°C, recombinant enzyme
0.028
scyllo-inositol 1,2,3,5-tetrakisphosphate
Rattus norvegicus
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weak inhibition, purified recombinant enzyme, IC50 value is 0.028 mM in absence of Ca2+
0.027
scyllo-inositol 1,2,3-trisphosphate
Rattus norvegicus
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purified recombinant enzyme, IC50 value is 0.027 mM in absence of Ca2+
0.039
scyllo-inositol 1,2,4,5-tetrakisphosphate
Rattus norvegicus
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weak inhibition, purified recombinant enzyme, IC50 value is 0.039 mM in absence of Ca2+
0.09
scyllo-inositol 1,3,5-trisphosphate
Rattus norvegicus
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purified recombinant enzyme, IC50 value is 0.090 mM in absence of Ca2+
0.00019
3',4',7,8-tetrahydroxyflavone
Rattus norvegicus
IP3K-C, maximal inhibition 75%
0.00019
3',4',7,8-tetrahydroxyflavone
Rattus norvegicus
recombinant enzyme IP3K-C fragment comprising calmodulin binding and catalytic domain
0.00029
3',4',7,8-tetrahydroxyflavone
Gallus gallus
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recombinant enzyme fragment comprising calmodulin binding domain
0.00061
3',4',7,8-tetrahydroxyflavone
Rattus norvegicus
recombinant enzyme IP3K-C fragment comprising catalytic domain
additional information
F-actin
Homo sapiens
the full length form of inositol 1,4,5-trisphosphate-3-kinase-A bundles F-actin in a concentration dependent manner, inhibition of the initial rate of gelsolin induces F-actin severing and the degree of bundling are half maximal at an similar concentration of about 300 nM, whereas inhibition of the rate of actin depolymerization after dilution to 100 nM actin is half maximal at about 30 nM, the much lower EC 50 for the latter effect may reflect the high affinity of enzyme for binding to F actin
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additional information
F-actin
Homo sapiens
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the full length form of inositol 1,4,5-trisphosphate-3-kinase-A bundles F-actin in a concentration dependent manner, inhibition of the initial rate of gelsolin induces F-actin severing and the degree of bundling are half maximal at an similar concentration of about 300 nM, whereas inhibition of the rate of actin depolymerization after dilution to 100 nM actin is half maximal at about 30 nM, the much lower EC 50 for the latter effect may reflect the high affinity of enzyme for binding to F actin
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additional information
additional information
Rattus norvegicus
RnIP3K-C including the calmodulin binding and the catalytic domain shows a 3-fold lower IC50 value for 3',4',7,8-tetrahydroxyflavone than RnIP3K including only the calmodulin binding domain. The maximum degree of inhibition is unchanged. Together with the finding that Ca2+-calmodulin partly reverses IP3K inhibition indicates a facilitating but not essential involvement of the calmodulin binding domain in inhibitor binding.
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