2.7.4.24: diphosphoinositol-pentakisphosphate 1-kinase

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For detailed information about diphosphoinositol-pentakisphosphate 1-kinase, go to the full flat file.

Reaction

Synonyms

ATP:5-diphospho-1D-myo-inositol-pentakisphosphate phosphotransferase, diphospho-myo-inositol pentakisphosphate 5-kinase, diphosphoinositol pentakisphosphate kinase, diphosphoinositol pentakisphosphate kinase 2, diphosphoinositol-pentakisphosphate 1/3-kinase, diphosphoinositol-pentakisphosphate kinase, EC 2.7.1.155, IP7 kinase, kinase (phosphorylating), diphosphoinositol 1,2,3,4,5-pentakisphosphate 5-, More, PP-InsP5 kinase, PP-IP5 kinase, PPIP5K, PPIP5K1, PPIP5K2, VIP, VIP1, VIP2

ECTree

     2 Transferases

         2.7 Transferring phosphorus-containing groups

             2.7.4 Phosphotransferases with a phosphate group as acceptor

                2.7.4.24 diphosphoinositol-pentakisphosphate 1-kinase

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Results	in table
16	Activating Compound
9099	AA Sequence
2	Application
1	CAS Registry Number
9	Cloned(Commentary)
7	Cofactor
3	Crystallization (Commentary)
4	Disease/ Diagnostics
8	General Information
9	IC50 Value
20	Inhibitors
6	kcat/KM [mM/s]
12	KM Value [mM]
1	Localization
4	Metals/Ions
7	Molecular Weight [Da]
18	Natural Substrates/ Products (Substrates)
20	Organism
1	Pathway
20	PDB ID
7	pH Optimum
1	pH Range
16	Protein Variants
7	Purification (Commentary)
2	Reaction
1	Reaction Type
20	Reference
12	Source Tissue
1	Specific Activity [micromol/min/mg]
3	Storage Stability
35	Substrates and Products (Substrate)
4	Subunits
54	Synonyms
1	Systematic Name
5	Temperature Optimum [°C]
1	Temperature Range [°C]
1	Temperature Stability [°C]
5	Turnover Number [1/s]

Crystallization

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Crystallization on EC 2.7.4.24 - diphosphoinositol-pentakisphosphate 1-kinase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Homo sapiens

O43314

721882

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

Homo sapiens

O43314

738042

the Lys248 side chain is rather centered on a position enabling an optimal pulling force applied to the leaving group along the reaction coordinate. The actions of Lys248 pulling forces are influenced by substrate binding. Residue Glu192 makes a specific contribution to the ability of PPIP5K2 to significantly reduce the entropy toll for the catch-and-pass reaction mechanism

Homo sapiens

O43314

762487