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Literature summary extracted from

  • Miller, G.J.; Hurley, J.H.
    Crystal structure of the catalytic core of inositol 1,4,5-trisphosphate 3-kinase (2004), Mol. Cell, 15, 703-711.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.127 expression of mutant cDNA fragment encoding for residues 185-459 of the catalytic domain of isozyme A as unlabeled or selenomethionine-labeled GST fusion proteins in Escherichia coli Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.127 purified recombinant unlabeled or selennomethionine-labeled mutant catalytic domain residues 185-459, 10 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 10 mM DTT, crystallization solution contains 2.2 M ammonium sulfate, 0.2 M sodium formate, 10 mM DTT, 10 mM ADP, 10 mM 1D-myo-inositol 1,3,4,5-tetrakisphosphate, and 10 mM MgCl2, cryoprotection of crystals by successive transfer into 5-15% glycerol in mother liquor, X-ray diffraction structure determination and analysis at 2.2 A resolution Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.127 D423N crystal structure determination and analysis Rattus norvegicus
2.7.1.127 L217M crystal structure determination and analysis Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.127 Mg2+
-
 Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.127 Rattus norvegicus
-
 isozyme A
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.127 unlabeled or selenomethionine-labeled recombinant residues 185-459 of the catalytic domain of isozyme A fused to GST from Escherichia coli by glutathione affinity chromatography, removal of the GST-tag by recombinant TEV protease, further purification by a second step of glutathione affinity chromatography, adsorption chromatography, and gel filtration Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.127 ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate catalytic core structure, substrate binding and catalytic mechanism, structure-function realtionship Rattus norvegicus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.127 ATP + 1D-myo-inositol 1,4,5-trisphosphate
-
 Rattus norvegicus ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
-
 ?
2.7.1.127 additional information the enzyme contains a catalytic domain and a 4-helix substrate binding domain, both are in an open conformation with respect to each other, thus substrate recognition and catalysis involve a dynamic conformational cycle Rattus norvegicus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.127 More the enzyme contains a catalytic domain and a 4-helix substrate binding domain, both are in an open conformation with respect to each other, thus substrate recognition and catalysis involve a dynamic conformational cycle Rattus norvegicus

Synonyms

EC Number Synonyms Comment Organism
2.7.1.127 inositol 1,4,5-trisphosphate 3-kinase
-
 Rattus norvegicus
2.7.1.127 IP3KA
-
 Rattus norvegicus
2.7.1.127 More the enzyme is a member of the protein kinase superfamily Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.127 ATP binding site structure Rattus norvegicus