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Information on EC 2.7.4.24 - diphosphoinositol-pentakisphosphate kinase and Organism(s) Homo sapiens and UniProt Accession O43314

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IUBMB Comments
This enzyme is activated by osmotic shock . Ins(1,3,4,5,6)P5, 1D-myo-inositol diphosphate tetrakisphosphate and 1D-myo-inositol bisdiphosphate triphosphate are not substrates .
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Select one or more organisms in this record:
This record set is specific for:
Homo sapiens
UNIPROT: O43314
Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
diphospho-myo-inositol pentakisphosphate 5-kinase, diphosphoinositol pentakisphosphate kinase, diphosphoinositol pentakisphosphate kinase 2, IP7 kinase, kinase (phosphorylating), diphosphoinositol 1,2,3,4,5-pentakisphosphate 5-, More, PP-InsP5 kinase, PP-IP5 kinase, PPIP5K, PPIP5K1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
diphospho-myo-inositol pentakisphosphate 5-kinase
-
-
-
-
diphosphoinositol pentakisphosphate kinase
diphosphoinositol pentakisphosphate kinase 2
288412
-
IP7 kinase
288411, 288412
-
kinase (phosphorylating), diphosphoinositol 1,2,3,4,5-pentakisphosphate 5-
-
-
-
-
PP-InsP5 kinase
PP-IP5 kinase
PPIP5K
PPIP5K1
288411
-
PPIP5K2
VIP
247
-
VIP1
288411
-
VIP2
288412
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
ATP:1D-myo-inositol-5-diphosphate-pentakisphosphate phosphotransferase
This enzyme is activated by osmotic shock [4]. Ins(1,3,4,5,6)P5, 1D-myo-inositol diphosphate tetrakisphosphate and 1D-myo-inositol bisdiphosphate triphosphate are not substrates [4].
CAS REGISTRY NUMBER
COMMENTARY hide
188929-01-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + 1,5-bis-diphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate
ATP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
show the reaction diagram
-
-
-
r
ADP + 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
show the reaction diagram
-
-
-
r
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
show the reaction diagram
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
show the reaction diagram
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
show the reaction diagram
-
-
-
?
ATP + 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
ADP + 1,5-bis-diphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate
show the reaction diagram
-
-
-
r
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP
1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP
show the reaction diagram
-
-
-
-
?
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
show the reaction diagram
-
-
-
-
?
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
show the reaction diagram
-
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL 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 5-diphosphate 1,2,3,4,6-pentakisphosphate
ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
show the reaction diagram
O43314
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
show the reaction diagram
O43314, Q6PFW1
-
-
-
?
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
show the reaction diagram
O43314
-
-
-
?
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP
1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP
show the reaction diagram
-
-
-
-
?
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
show the reaction diagram
-
-
-
-
?
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
show the reaction diagram
-
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,5-O-benzyl-myo-inositol 1,3,4,6-tetrakisphosphate
activates the ATP hydrolysis activity and inhibits the PPIP5K2 activity and InsP6 kinase activity, and the 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme. The compound can inhibit inositol phosphate kinase activity without occupying the catalytic site
2-O-benzyl-5-(phosphonoacetic acid ester)-1D-myo-inositol tetrakisphosphate
-
2-O-benzyl-5-O-alpha-phosphonoacetyl-myo-inositol 1,3,4,6-tetrakisphosphate
stimulates ATP hydrolysis 9fold, but inhibits 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme. The compound can inhibit inositol phosphate kinase activity without occupying the catalytic site
2-O-benzyl-5-O-diphosphate-myo-inositol 1,3,4,6-tetrakisphosphate
activates ATP hydrolysis activity but inhibits 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme
2-O-benzyl-myo-inositol 1,2,3,4,6-pentakisphosphate
activates ATP hydrolysis activity but inhibits 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme
5-(phosphonoacetic acid ester)-1D-myo-inositol pentakisphosphate
most potent inhibitor
5-(phosphonoacetic acid ester)-1D-myo-inositol tetrakisphosphate
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5-O-alpha-diphosphate-myo-inositol 1,3,4,6-tetrakisphosphate
activates ATP hydrolysis activity but inhibits 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme
5-O-alpha-phosphonoacetyl-myo-inositol 1,2,3,4,6-pentakisphosphate
stimulates ATP hydrolysis 5fold, but inhibits 1,5-[PP]2-InsP4 dephosphorylation activity of the enzyme
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,5-O-benzyl-myo-inositol 1,3,4,6-tetrakisphosphate
activates the ATP hydrolysis activity and inhibits the InsP6 kinase activity of the enzyme
2-O-aminoethyl-myo-inositol 1,2,3,4,6-pentakisphosphate
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2-O-benzoyl-myo-inositol 1,2,3,4,6-pentakisphosphate
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2-O-benzyl-5-O-alpha-phosphonoacetyl-myo-inositol 1,3,4,6-tetrakisphosphate
stimulates ATP hydrolysis 9fold
2-O-benzyl-5-O-diphosphate-myo-inositol 1,3,4,6-tetrakisphosphate
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2-O-benzyl-myo-inositol 1,2,3,4,6-pentakisphosphate
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2-O-butanoyl-myo-inositol 1,2,3,4,6-pentakisphosphate
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5-O-alpha-diphosphate-myo-inositol 1,3,4,6-tetrakisphosphate
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5-O-alpha-phoshonoacetyl-myo-inositol 1,3,4,6-tetrakisphosphate
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5-O-alpha-phosphonoacetyl-myo-inositol 1,2,3,4,6-pentakisphosphate
stimulates ATP hydrolysis 5fold
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000022
1,5-bis-diphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
0.00011
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 m MKCl, at 37°C
0.00019
1D-myo-inositol 5-diphosphate pentakisphosphate
pH 6.2, 37°C, VIP2
0.00006
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
0.0052 - 0.9
ADP
0.022
ATP
isoform PPIP5K2, using 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate as cosubstrate, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
0.0001
1D-myo-inositol 5-diphosphate pentakisphosphate
pH 6.2, 37°C, VIP1
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
1,5-bis-diphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
0.002
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 m MKCl, at 37°C
38
1D-myo-inositol 5-diphosphate pentakisphosphate
pH 6.2, 37°C, VIP2
0.13
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
4
1D-myo-inositol 5-diphosphate pentakisphosphate
pH 6.2, 37°C, VIP1
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8500
1,5-bis-diphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
17
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 m MKCl, at 37°C
2200
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate
isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
0.037 - 0.21
ADP
5.9
ATP
isoform PPIP5K2, using 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate as cosubstrate, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00017
2,5-O-benzyl-myo-inositol 1,3,4,6-tetrakisphosphate
Homo sapiens
O43314
inhibition of the 1,5-[PP]2-InsP4 dephosphorylation, pH 7.0, 37°C
0.391
2-O-benzyl-5-(phosphonoacetic acid ester)-1D-myo-inositol tetrakisphosphate
Homo sapiens
O43314
pH and temperature not specified in the publication
0.00042
2-O-benzyl-5-O-alpha-phosphonoacetyl-myo-inositol 1,3,4,6-tetrakisphosphate
Homo sapiens
O43314
inhibition of the 1,5-[PP]2-InsP4 dephosphorylation, pH 7.0, 37°C
0.0005
2-O-benzyl-5-O-diphosphate-myo-inositol 1,3,4,6-tetrakisphosphate
Homo sapiens
O43314
inhibition of the 1,5-[PP]2-InsP4 dephosphorylation, pH 7.0, 37°C
0.00044
2-O-benzyl-myo-inositol 1,2,3,4,6-pentakisphosphate
Homo sapiens
O43314
inhibition of the 1,5-[PP]2-InsP4 dephosphorylation, pH 7.0, 37°C
0.129
5-(phosphonoacetic acid ester)-1D-myo-inositol pentakisphosphate
Homo sapiens
O43314
pH and temperature not specified in the publication
1.386
5-(phosphonoacetic acid ester)-1D-myo-inositol tetrakisphosphate
Homo sapiens
O43314
pH and temperature not specified in the publication
0.0024
5-O-alpha-diphosphate-myo-inositol 1,3,4,6-tetrakisphosphate
Homo sapiens
O43314
inhibition of the 1,5-[PP]2-InsP4 dephosphorylation, pH 7.0, 37°C
0.00014
5-O-alpha-phosphonoacetyl-myo-inositol 1,2,3,4,6-pentakisphosphate
Homo sapiens
O43314
inhibition of the 1,5-[PP]2-InsP4 dephosphorylation, pH 7.0, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 7.5
assay at
7.2
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
positional specificity of the mammalian and yeast VIP/diphosphoinositol pentakisphosphate kinase family of inositol phosphate kinases, overview. The mammalian and yeast VIP/PPIP5K family enzymes phosphorylate the 1/3-position of the inositol ring in vitro and in vivo, phylogenetic variability within the crown taxa in the structures of inositol pyrophosphates, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
Sequence
VIP2_HUMAN
1243
0
140407
Swiss-Prot
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
138000
about, isozyme PPIP5K2, mass spectrometry
160000
about, isozyme PPIP5K1, mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme contains a putative ATP-grasp kinase domain
CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
N-terminally truncated PPIP5K2 kinase mutant, residues 41-366, hanging drop vapor diffusion against a well buffer of 12% w/v PEG 3350, 20 mM MgCl2, 0.1 M HEPES, pH 7.0, 0,1 mM AMP-PNP, and 2 mM CdCl2 at 4°C, 3 days, 4°C, X-ray diffraction structure determination and analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E192G
site-directed mutagenesis
E192Q
site-directed mutagenesis
K103A
site-directed mutagenesis
K213A
site-directed mutagenesis
K248A
the mutant shows a reduction in 1D-myo-inositol hexakisphosphate-stimulated ATPase activity of isofom PPIP5K2. The mutant shows a significant reduction in the rate of 1D-myo-inositol phosphate-independent ATPase activity of isofom PPIP5K2
K54A
site-directed mutagenesis
R213A
the mutant shows a reduction in 1D-myo-inositol hexakisphosphate-stimulated ATPase activity of isofom PPIP5K2
D332A
catalytically inactive mutant of isozyme PPIP5K1
additional information
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
GSTrap HP column chromatography
recombinant wild-type and truncated mutant enzymes
recombinant FLAG-tagged or untagged isozymes PPIP5K1 and PPIP5K2 from HEK-293 cells and isozyme PPIP5K1 from Escherichia coli, respectively
recombinant GST-tagged wild-type Saccharomyces cerevisiae Vip1 kinase domain and mutant Vip1 fused to human GSTIP6K1 from bacteria
-
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
gene VIP2, DNA and amino acid sequence determination and analysis, functional expression of CFP- or GST-tagged VIP2 in HEK-293T cells
recombinant expression of wild-type and mutant enzymes
expression of wild-type Saccharomyces cerevisiae Vip1 kinase domain and of mutant Vip1 fused to human GSTIP6K1 as GST-tagged proteins in bacteria
-
functional overexpression of isozymes PPIP5K1 and PPIP5K2 in HEK-293 cells, expression of isozyme PPIP5K1 in Escherichia coli
gene VIP1, DNA and amino acid sequence determination and analysis, VIP1 expression in mutant yeast, functional expression of CFP- or GST-tagged VIP1 in HEK-293T cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fridy, P.C.; Otto, J.C.; Dollins, D.E.; York, J.D.
Cloning and characterization of two human VIP1-like inositol hexakisphosphate and diphosphoinositol pentakisphosphate kinases
J. Biol. Chem.
282
30754-30762
2007
Homo sapiens, Homo sapiens (O43314), Homo sapiens (Q6PFW1)
Manually annotated by BRENDA team
Choi, J.H.; Williams, J.; Cho, J.; Falck, J.R.; Shears, S.B.
Purification, sequencing, and molecular identification of a mammalian PP-InsP5 kinase that is activated when cells are exposed to hyperosmotic stress
J. Biol. Chem.
282
30763-30775
2007
Homo sapiens, Homo sapiens (Q6PFW1), Rattus norvegicus (P0C644)
Manually annotated by BRENDA team
Lin, H.; Fridy, P.C.; Ribeiro, A.A.; Choi, J.H.; Barma, D.K.; Vogel, G.; Falck, J.R.; Shears, S.B.; York, J.D.; Mayr, G.W.
Structural analysis and detection of biological inositol pyrophosphates reveal that the family of VIP/diphosphoinositol pentakisphosphate kinases are 1/3-kinases
J. Biol. Chem.
284
1863-1872
2009
Homo sapiens, Saccharomyces cerevisiae
Manually annotated by BRENDA team
Weaver, J.D.; Wang, H.; Shears, S.B.
The kinetic properties of a human PPIP5K reveal that its kinase activities are protected against the consequences of a deteriorating cellular bioenergetic environment
Biosci. Rep.
33
e00022
2013
Homo sapiens, Homo sapiens (O43314)
Manually annotated by BRENDA team
Riley, A.M.; Wang, H.; Weaver, J.D.; Shears, S.B.; Potter, B.V.
First synthetic analogues of diphosphoinositol polyphosphates: interaction with PP-InsP5 kinase
Chem. Commun. (Camb. )
48
11292-11294
2012
Homo sapiens (O43314)
Manually annotated by BRENDA team
Wang, H.; Godage, H.Y.; Riley, A.M.; Weaver, J.D.; Shears, S.B.; Potter, B.V.
Synthetic inositol phosphate analogs reveal that PPIP5K2 has a surface-mounted substrate capture site that is a target for drug discovery
Chem. Biol.
21
689-699
2014
Homo sapiens (O43314)
Manually annotated by BRENDA team
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