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1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP
1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
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
-
-
-
r
ADP + 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
-
-
-
r
ADP + diphosphoinositol pentakisphosphate
ATP + ?
-
enzyme has ATP synthase activity
-
-
?
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
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
-
-
-
?
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
-
-
-
r
ATP + 5-diphospho-1D-myo-inositol pentakisphosphate
ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
ATP + 5-diphospho-1D-myo-inositol-pentakisphosphate
ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
additional information
?
-
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP

1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP
-
-
-
-
?
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP
1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP
-
-
-
-
?
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP

3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
-
-
-
-
?
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
-
-
-
-
?
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP

3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
-
-
-
-
?
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
-
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate

ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
(PP)2-InsP4 synthesis pathway, overview
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
(PP)2-InsP4 synthesis pathway, overview
-
-
?
ATP + 5-diphospho-1D-myo-inositol pentakisphosphate

ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
-
-
-
-
?
ATP + 5-diphospho-1D-myo-inositol pentakisphosphate
ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
-
bis(diphospho)-1D-myo-inositol tetrakisphosphate specifically impedes protein trafficking, no regulation by extracellular signal-regulated kinase or phopholipase D
-
-
?
ATP + 5-diphospho-1D-myo-inositol-pentakisphosphate

ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
-
-
-
-
?
ATP + 5-diphospho-1D-myo-inositol-pentakisphosphate
ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
-
-
-
?
ATP + 5-diphospho-1D-myo-inositol-pentakisphosphate
ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
-
-
-
-
?
additional information

?
-
VIP1 also performs the reaction of EC 2.7.4.21
-
-
-
additional information
?
-
VIP1 also performs the reaction of EC 2.7.4.21
-
-
-
additional information
?
-
VIP2 also performs the reaction of EC 2.7.4.21
-
-
-
additional information
?
-
VIP2 also performs the reaction of EC 2.7.4.21
-
-
-
additional information
?
-
-
recombinant Vip1 kinase domain catalyzes 5-diphospho-1D-myo-inositol (1,2,3,4,6)pentakisphosphate formation from inositol hexakisphosphate. NMR substrate and product analysis, overview
-
-
-
additional information
?
-
the bifunctional enzyme also catalyzes the reaction of EC 2.7.4.21, InsP6 kinase. The enzyme exhibits an unusual, nonproductive, substrate-stimulated ATPase activity, that is stimulated by the natural substrates and by 5-O-alpha-phosphonoacetyl-myo-inositol 1,2,3,4,6-pentakisphosphate and 2-O-benzyl-5-O-alpha-phosphonoacetyl-myo-inositol 1,3,4,6-tetrakisphosphate. It also shows 1,5-[PP]2-InsP4 dephosphorylation activity. The enzyme has two adjacent ligand-binding sites, the architecture of this second ligand-binding site is represented by a deep cleft, which is walled on one side by K53, K54, and K103. The opposite face is formed from R213, and a loop created from residues E192 to H194
-
-
-
additional information
?
-
-
recombinant Vip1 kinase domain catalyzes 5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate formation from inositol hexakisphosphate. NMR substrate and product analysis, overview
-
-
-
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1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP
1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
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
O43314
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
O43314
-
-
-
?
ATP + 5-diphospho-1D-myo-inositol pentakisphosphate
ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
-
bis(diphospho)-1D-myo-inositol tetrakisphosphate specifically impedes protein trafficking, no regulation by extracellular signal-regulated kinase or phopholipase D
-
-
?
ATP + 5-diphospho-1D-myo-inositol-pentakisphosphate
ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
-
-
-
-
?
additional information
?
-
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP

1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP
-
-
-
-
?
1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ATP
1,5-bisdiphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate + ADP
-
-
-
-
?
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP

3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
-
-
-
-
?
3-diphospho-1D-myo-inositol 1,2,4,5,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
-
-
-
-
?
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP

3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
-
-
-
-
?
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
-
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate

ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
O43314, Q6PFW1
-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
Q6PFW1
(PP)2-InsP4 synthesis pathway, overview
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
P0C644
(PP)2-InsP4 synthesis pathway, overview
-
-
?
additional information

?
-
O43314
VIP1 also performs the reaction of EC 2.7.4.21
-
-
-
additional information
?
-
Q6PFW1
VIP1 also performs the reaction of EC 2.7.4.21
-
-
-
additional information
?
-
O43314
VIP2 also performs the reaction of EC 2.7.4.21
-
-
-
additional information
?
-
Q6PFW1
VIP2 also performs the reaction of EC 2.7.4.21
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
-
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
chlorpromazine
-
inhibition in vivo
F-
-
50% inhibition at 0.03 mM
genistein
-
rapid inhibition in vivo
N-(6-Aminohexyl)-5-chloro-1-naphthalenesulfonamide
-
i.e. W-7, rapid inhibition in vivo
additional information

-
isoform PPIP5K2 is insensitive to physiological changes in either [AMP] or [ATP]/[ADP] ratios
-
additional information
isoform PPIP5K2 is insensitive to physiological changes in either [AMP] or [ATP]/[ADP] ratios
-
additional information
synthesis and effects of inositol phosphates and analogues upon ATPase activity, overview. The compounds are also inhibitors of [PP]2-InsP4 dephosphorylation. Binding structures, overview
-
additional information
-
no in vivo inhibition by wortmannin, SB203580, i.e. 4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)1H-imidazole, PD98059, i.e. 2'-amino-3'-methoxyflavone, rapamycin, dephostatin, okadaic acid, herbimycin, K-252a, i.e. methyl-(9S,12R)-epoxy-1H-diinodolo[1,2,3-fg:3',2',1'-kI]pyrrolo[3,4-i][1,6]benzodiazocine-2,3,9,10,11,12-hexahydro-(10R)-hydroxy-9-methyl-1-oxo-10-carboxylate, and KN-93, i.e. 2-[N-(4-chlorocinnamoyl)-N-methylbenzylamine]
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
2-O-benzoyl-myo-inositol 1,2,3,4,6-pentakisphosphate
-
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
-
2-O-benzyl-myo-inositol 1,2,3,4,6-pentakisphosphate
-
2-O-butanoyl-myo-inositol 1,2,3,4,6-pentakisphosphate
-
5-O-alpha-diphosphate-myo-inositol 1,3,4,6-tetrakisphosphate
-
5-O-alpha-phoshonoacetyl-myo-inositol 1,3,4,6-tetrakisphosphate
-
5-O-alpha-phosphonoacetyl-myo-inositol 1,2,3,4,6-pentakisphosphate
stimulates ATP hydrolysis 5fold
monoperoxo(picolinato)oxovanadate(V)
-
15fold activation
sorbitol
-
rapid activation in vivo
Sucrose
-
rapid activation in vivo
additional information

activation of recombinant PPIP5K1 by hyperosmotic stress in HEK-293 cells
-
additional information
synthesis and effects of inositol phosphates and analogues upon ATPase activity, overview. The compounds are also inhibitors of [PP]2-InsP4 dephosphorylation. Binding structures, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
0.0001 - 0.00019
1D-myo-inositol 5-diphosphate pentakisphosphate
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
0.7
diphosphoinositol pentakisphosphate
-
pH 6.8, 37°C
1.94
diphosphoinositol tetrakisphosphate
-
pH 6.8, 37°C
0.0001
1D-myo-inositol 5-diphosphate pentakisphosphate

pH 6.2, 37°C, VIP1
0.00019
1D-myo-inositol 5-diphosphate pentakisphosphate
pH 6.2, 37°C, VIP2
0.0052
ADP

isoform PPIP5K2, using 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate as cosubstrate, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
0.9
ADP
isoform PPIP5K2, using 1,5-bis-diphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate as cosubstrate, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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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
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
0.037
ADP

isoform PPIP5K2, using 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate as cosubstrate, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
0.21
ADP
isoform PPIP5K2, using 1,5-bis-diphospho-1D-myo-inositol 2,3,4,6-tetrakisphosphate as cosubstrate, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Voglmaier, S.M.; Bembenek, M.E.; Kaplin, A.I.; Dorman, G.; Olszewski, J.D.; Prestwich, G.D.; Snyder, S.H.
Purified inositol hexakisphosphate kinase is an ATP synthase: diphosphoinositol pentakisphosphate as a high-energy phosphate donor
Proc. Natl. Acad. Sci. USA
93
4305-4310
1996
Rattus norvegicus
brenda
Huang, C.F.; Voglmaier, S.M.; Bembenek, M.E.; Saiardi, A.; Snyder, S.H.
Identification and purification of diphosphoinositol pentakisphosphate kinase, which synthesizes the inositol pyrophosphate bis(diphospho)inositol tetrakisphosphate
Biochemistry
37
14998-15004
1998
Rattus norvegicus
brenda
Shears, S.B.; Ali, N.; Craxton, A.; Bembenek, M.E.
Synthesis and metabolism of bis-diphosphoinositol tetrakisphosphate in vitro and in vivo
J. Biol. Chem.
270
10489-10497
1995
Rattus norvegicus
brenda
Safrany, S.T.
Protocols for regulation and study of diphosphoinositol polyphosphates
Mol. Pharmacol.
66
1585-1591
2004
Mesocricetus auratus
brenda
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)
brenda
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)
brenda
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
brenda
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)
brenda
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)
brenda
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)
brenda