Literature summary for 2.7.1.159 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.

Search for more literature for 2.7.1.159

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

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

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Entamoeba histolytica

Natural Substrates/ Products (Substrates)

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

Organism

Organism	UniProt	Comment	Textmining
Entamoeba histolytica	Q9XYQ1	-	-

Purification (Commentary)

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

Reaction

Reaction	Comment	Organism	Reaction ID
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
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)

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Entamoeba histolytica