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Literature summary extracted from

  • Miller, G.J.; Wilson, M.P.; Majerus, P.W.; Hurley, J.H.
    Specificity determinants in inositol polyphosphate synthesis: crystal structure of inositol 1,3,4-trisphosphate 5/6-kinase (2005), Mol. Cell, 18, 201-212.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.159 expression of GST-tagged wild-type enzyme and of mutant enzymes in Escherichia coli Entamoeba histolytica

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.159 purified recombinant enzyme free or in complex with ATP analogue AMP-PCP and substrate inositol-1,3,4-trisphosphate in presence of Mg2+, 30 mg/ml protein in 25 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 10 mM DTT, mixed with a solution containing 20% PEG 3000, 0.1 M Tris-HCl, pH 7.5, and 0.1 M Ca(OAc)2, several months, crystals are seeded into sitting drops of 15 mg/ml protein, 25% PEG 3350, 5% PEG 400, 0.1 M Bis-Tris, pH 5.5, 10 mM DTT, and 10 mM L-cysteine, with or without ligands added as 10 mM AMP-PCP, 10 mM MgCl2, and 5 mM inositol-1,3,4-trisphosphate, direct X-ray diffraction analysis after this step or further seeding adding ADP and other ligands, overview, X-ray diffraction structure determination and analysis at 1.2-2.0 A resolution Entamoeba histolytica

Protein Variants

EC Number Protein Variants Comment Organism
2.7.1.159 additional information construction of diverse mutants and analysis of the function of the residues in catalysis and substrate binding, overview Entamoeba histolytica

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.159 Mg2+
-
 Entamoeba histolytica

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.1.159 ATP + 1D-myo-inositol-1,3,4-trisphosphate Entamoeba histolytica
-
 ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
 ?
2.7.1.159 ATP + 1D-myo-inositol-1,3,4-trisphosphate Entamoeba histolytica
-
 ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.159 Entamoeba histolytica Q9XYQ1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.159 recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography and gel filtration Entamoeba histolytica

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.159 ATP + 1D-myo-inositol-1,3,4-trisphosphate = ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate determination of substrate binding sites, catalytic reaction mechanism Entamoeba histolytica
a
2.7.1.159 ATP + 1D-myo-inositol-1,3,4-trisphosphate = ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate determination of substrate binding sites, catalytic reaction mechanism Entamoeba histolytica
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.159 ATP + 1D-myo-inositol-1,3,4-trisphosphate
-
 Entamoeba histolytica ADP + 1D-myo-inositol-1,3,4,5-tetrakisphosphate
-
 ?
2.7.1.159 ATP + 1D-myo-inositol-1,3,4-trisphosphate
-
 Entamoeba histolytica ADP + 1D-myo-inositol-1,3,4,6-tetrakisphosphate
-
 ?
2.7.1.159 additional information the enzyme shows multiple activities Entamoeba histolytica ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.159 IP56K
-
 Entamoeba histolytica
2.7.1.159 More the enzyme belongs to the ATP-grasp family Entamoeba histolytica

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.159 37
-
 assay at Entamoeba histolytica

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.159 7.2
-
 assay at Entamoeba histolytica

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.159 ATP
-
 Entamoeba histolytica