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Information on EC 2.7.4.24 - diphosphoinositol-pentakisphosphate kinase
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2.7.4.24 diphosphoinositol-pentakisphosphate kinaseIUBMB 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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Word Map
- 2.7.4.24
- pyrophosphate
- polyphosphate
-
pp-insps
- hexakisphosphate
-
bisdiphosphoinositol
- tetrakisphosphate
-
pleckstrin
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ptdins3,4,5p3
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campaigns
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ptdins3,4,5p3-binding
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interactors
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telomere
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hyperosmotic
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
ppip5k1, ppip5k, ip7 kinase, diphosphoinositol pentakisphosphate kinase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
diphospho-myo-inositol pentakisphosphate 5-kinase
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-
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diphosphoinositol pentakisphosphate kinase
kinase (phosphorylating), diphosphoinositol 1,2,3,4,5-pentakisphosphate 5-
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-
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PP-InsP5 kinase
PP-IP5 kinase
PPIP5K
PPIP5K2
VIP
additional information
diphosphoinositol pentakisphosphate kinase
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-
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PP-IP5 kinase
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additional information
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the enzyme belongs to the VIP/diphosphoinositol pentakisphosphate kinase, PPIP5K, family of inositol phosphate kinases
additional information
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the enzyme belongs to the VIP/diphosphoinositol pentakisphosphate kinase, PPIP5K, family of inositol phosphate kinases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
; (1)
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-
-
ATP + 1D-myo-inositol hexakisphosphate = ADP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate
(2)
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
-
-
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PATHWAY SOURCE
PATHWAYS
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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].
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CAS REGISTRY NUMBER
COMMENTARY
188929-01-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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-
r
ADP + 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate
ATP + 1D-myo-inositol hexakisphosphate
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-
r
ADP + diphosphoinositol pentakisphosphate
ATP + ?
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enzyme has ATP synthase activity
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-
?
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
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-
-
?
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
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-
-
?
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
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-
-
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
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
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-
-
-
?
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
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-
-
-
?
5-diphospho-1D-myo-inositol 1,2,3,4,6-pentakisphosphate + ATP
3,5-bisdiphospho-1D-myo-inositol 1,2,4,6-tetrakisphosphate + ADP
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-
-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
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-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
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-
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?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
(PP)2-InsP4 synthesis pathway, overview
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-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
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-
-
?
ATP + 1D-myo-inositol 5-diphosphate pentakisphosphate
ADP + 1D-myo-inositol bisdiphosphate tetrakisphosphate
(PP)2-InsP4 synthesis pathway, overview
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-
?
ATP + 5-diphospho-1D-myo-inositol pentakisphosphate
ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
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-
-
-
?
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
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-
?
ATP + 5-diphospho-1D-myo-inositol-pentakisphosphate
ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
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-
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?
ATP + 5-diphospho-1D-myo-inositol-pentakisphosphate
ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
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-
-
?
ATP + 5-diphospho-1D-myo-inositol-pentakisphosphate
ADP + bis(diphospho)-1D-myo-inositol tetrakisphosphate
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-
?
additional information
?
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VIP1 also performs the reaction of EC 2.7.4.21
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additional information
?
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VIP1 also performs the reaction of EC 2.7.4.21
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additional information
?
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VIP2 also performs the reaction of EC 2.7.4.21
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additional information
?
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VIP2 also performs the reaction of EC 2.7.4.21
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additional information
?
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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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additional information
?
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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
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-
additional information
?
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-
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
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-
-
?
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
-
-
-
-
?
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
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-
-
?
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
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-
-
additional information
?
-
Q6PFW1
VIP2 also performs the reaction of EC 2.7.4.21
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-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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-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
N-(6-Aminohexyl)-5-chloro-1-naphthalenesulfonamide
-
i.e. W-7, rapid inhibition in vivo
additional information
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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
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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]
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
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-benzyl-5-O-alpha-phosphonoacetyl-myo-inositol 1,3,4,6-tetrakisphosphate
stimulates ATP hydrolysis 9fold
5-O-alpha-phosphonoacetyl-myo-inositol 1,2,3,4,6-pentakisphosphate
stimulates ATP hydrolysis 5fold
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
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Hearing Loss
Mutations in Diphosphoinositol-Pentakisphosphate Kinase PPIP5K2 are associated with hearing loss in human and mouse.
Infection
Human genome-wide RNAi screen identifies an essential role for inositol pyrophosphates in Type-I interferon response.
Influenza, Human
Human genome-wide RNAi screen identifies an essential role for inositol pyrophosphates in Type-I interferon response.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
0.00006
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
0.0001
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
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
38
1D-myo-inositol 5-diphosphate pentakisphosphate
pH 6.2, 37°C, VIP2
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
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
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
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
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
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
7.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
-
the yeast VIP/PPIP5K family enzymes phosphorylate the 1/3-position of the inositol ring in vitro and in vivo, and convert inositol hexakisphosphate to 1/3-diphosphoinositol pentakisphosphate with determination of unequivocally 1/3,5-(PP)2-IP4 is the isomeric structure of the bis-diphosphoinositol tetrakisphosphate
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
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
Show AA Sequence and Transmembrane Helices (2438 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
160000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the enzyme contains a putative ATP-grasp kinase domain
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
R213A
the mutant shows a reduction in 1D-myo-inositol hexakisphosphate-stimulated ATPase activity of isofom PPIP5K2
additional information
additional information
VIP1 expression in mutant yeast restores IP7 synthesis
additional information
VIP1 expression in mutant yeast restores IP7 synthesis
additional information
-
construction of full-length recombinant human GSTIP6K1, plus either Saccharomyces cerevisiae GST fusion constructs comprising residues 1-387 of the human VIP1/PPIP5K1 kinase domain or residues 1-535 of the ScVip1 kinase domain
additional information
construction of an N-terminally truncated mutant PPIP5K2KD comprising residues 41-366
additional information
-
construction of full-length recombinant human GSTIP6K1, plus either GST fusion constructs comprising residues 1-387 of the human VIP1/PPIP5K1 kinase domain or residues 1-535 of the ScVip1 kinase domain
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
native PPIP5K1 from rat brain by anion exchange and heparin affinity chromatography, followed by nickel affinity chromatography and sucrose gradient centrifugation
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
recombinant GST-tagged wild-type Saccharomyces cerevisiae Vip1 kinase domain and mutant Vip1 fused to human GSTIP6K1 from bacteria
-
recombinant GST-tagged wild-type Saccharomyces cerevisiae Vip1 kinase domain and mutant Vip1 fused to human GSTIP6K1 from bacteria
-
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CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
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; gene VIP2, DNA and amino acid sequence determination and analysis, functional expression of CFP- or GST-tagged VIP2 in HEK-293T cells
expression of wild-type Saccharomyces cerevisiae Vip1 kinase domain and of mutant Vip1 fused to human GSTIP6K1 as GST-tagged proteins in bacteria
-
expression of wild-type Saccharomyces cerevisiae Vip1 kinase domain and of mutant Vip1 fused to human GSTIP6K1 as GST-tagged proteins in bacteria
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
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